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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
- pan locus tag?: SAUPAN004200000
- symbol: SACOL1661
- pan gene symbol?: —
- synonym:
- product: acetyl-CoA carboxylase, biotin carboxylase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
- symbol: SACOL1661
- product: acetyl-CoA carboxylase, biotin carboxylase
- replicon: chromosome
- strand: -
- coordinates: 1689999..1691360
- length: 1362
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3236534 NCBI
- RefSeq: YP_186501 NCBI
- BioCyc: see SACOL_RS08475
- MicrobesOnline: 913110 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1321ATGCTTCGTTGTTTAATTGCGAACAGAGGTGAAATTGCTGTAAGGATTATAAGAGCTTGC
AGAGAATATGGGATTGAAACTGTAGCAGTTTATGCAAAAGGGGACGAGCAAAGCTTGCAT
GTACATTTAGCAGATCAAGCTATATGTATTGGGGAAGCTAATGCTTTAGATAGTTATTTA
AATATTGACCGCATCATATCTGCTGCACAAATCACTGGTGCTAATGCAATTCACCCAGGA
TATGGCTTTTTATCAGAATCAACAAAATTTGCTCAAACCGTTGAGGAACAAGGCATAGCG
TTTATAGGGCCTACTAAAAAAACGATGGAAATGATGGGGGATAAAATAACAGCAAGACAA
ACAGTTCATCATGCAGGTGTTCCTGTGATTCCAGGATCAAATGGTGCTGTGAATCATGTG
TCTGAAATTGAGAATCTTGCCAAAGACATCGGTTATCCAGTTGTTATCAAAGCTGCCAGT
GGCGGTGGTGGTAAAGGTATACGTATTGTAAAGAAAGCTGAAGATTTAGAAAAGGCATTT
AAAGAAGCTAAAAGTGAAGGAAAAAAATACTTTGATGATGATCGTGTTTATGTTGAGGCT
TTTATACCTGTTGCAAAACATGTTGAAGTTCAAGTTATGGGAGATGGGCAGGATAATTAT
GTACATTTAGGGGAACGTGATTGTTCTGTACAACGTAAAAATCAAAAATTAATCGAAGAA
TCTCCTTGTGCAGCATTAACTGAAGAAAGACGACAACAAATATGTAACGATGCTGTTAAA
GTTGCACGTGCAGCAAATTATAGAAGTGCAGGTACGATTGAATTTTTAGTAACTGATACC
GCACATTACTTTATTGAAATGAATGCTCGAATACAAGTTGAACATACTGTTACAGAGATG
CGAGCAGAACGTGATTTGGTTGCAGCACAACTGTATTTATTGGAACATAATCATTTACCT
TTTTCACAAAGCGATATTCAATTTAATGGTCATGTGATAGAAGCGAGAATAAATGCCGAA
AATCCTGAAAAGAAATTTCAACCAACACCAGGTAAAGTGACAGCGTTACATTTACCTCAA
GGCTTTAATGTGCGAGTCGATTCTTTACTATATCACGGTTATCAAGTTTCACCATATTAT
GATTCTTTAGTAGCTAAAGTAATTGTAAAATCTCATGATAGAGCTTCAGCAATTGATAAG
TTGAAAGTCACCTTAGATGAAATGGTGATAGATGGATTTTCTACAACTGCCGATTTTTTA
TATGCAGTTTTAAATTATCCACTATATCGTGATGGAGATGCAAAAGATGTTGATATTAAA
TTTTTAGAAAAACATCAAATTGTTAAAGGGGTGGAATTATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1661 [new locus tag: SACOL_RS08475 ]
- symbol: SACOL1661
- description: acetyl-CoA carboxylase, biotin carboxylase
- length: 453
- theoretical pI: 6.36863
- theoretical MW: 50223.8
- GRAVY: -0.237086
⊟Function[edit | edit source]
- TIGRFAM: Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 601.9)Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 508.4)Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 502.1)and 11 morePurines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, large subunit (TIGR01369; EC 6.3.5.5; HMM-score: 56.1)Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan D-alanine--D-alanine ligase (TIGR01205; EC 6.3.2.4; HMM-score: 54.2)Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylglycinamide formyltransferase 2 (TIGR01142; EC 2.1.2.-; HMM-score: 49.5)Cellular processes Biosynthesis of natural products cyanophycin synthetase (TIGR02068; EC 6.3.2.29,6.3.2.30; HMM-score: 47.5)Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylaminoimidazole carboxylase, ATPase subunit (TIGR01161; EC 4.1.1.21; HMM-score: 43.3)Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylamine--glycine ligase (TIGR00877; EC 6.3.4.13; HMM-score: 40.4)alpha-L-glutamate ligase, RimK family (TIGR00768; EC 6.3.2.-; HMM-score: 37.8)lysine biosynthesis enzyme LysX (TIGR02144; HMM-score: 36.1)alpha-L-glutamate ligase homolog (TIGR02291; HMM-score: 18.9)Amino acid biosynthesis Other pyrrolysine biosynthesis protein PylC (TIGR03909; HMM-score: 16.1)Biosynthesis of cofactors, prosthetic groups, and carriers Other coenzyme gamma-F420-2:alpha-L-glutamate ligase (TIGR04443; EC 6.3.2.32; HMM-score: 13.6)
- TheSEED :
- Biotin carboxylase (EC 6.3.4.14)
- PFAM: ATP-grasp (CL0179) CPSase_L_D2; Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786; HMM-score: 216.8)and 13 morePreATP-grasp (CL0483) Biotin_carb_N; Biotin carboxylase, N-terminal domain (PF00289; HMM-score: 151.7)Hybrid (CL0105) Biotin_carb_C; Biotin carboxylase C-terminal domain (PF02785; HMM-score: 122.4)ATP-grasp (CL0179) Dala_Dala_lig_C; D-ala D-ala ligase C-terminus (PF07478; HMM-score: 49.1)ATPgrasp_Ter; ATP-grasp in the biosynthetic pathway with Ter operon (PF15632; HMM-score: 43.9)ATP-grasp; ATP-grasp domain (PF02222; HMM-score: 40.1)ATP-grasp_3; ATP-grasp domain (PF02655; HMM-score: 36.5)ATPgrasp_ST; Sugar-transfer associated ATP-grasp (PF14397; HMM-score: 27.9)RimK; RimK-like ATP-grasp domain (PF08443; HMM-score: 21.9)GARS_A; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain (PF01071; HMM-score: 20.4)ATP-grasp_4; ATP-grasp domain (PF13535; HMM-score: 20)ATP-grasp_5; ATP-grasp domain (PF13549; HMM-score: 14.6)Chelatase (CL0043) Oxidored_nitro; Nitrogenase component 1 type Oxidoreductase (PF00148; HMM-score: 13.1)no clan defined DUF3906; Protein of unknown function (DUF3906) (PF13046; HMM-score: 12.7)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 7.5
- Cytoplasmic Membrane Score: 1.15
- Cellwall Score: 0.62
- Extracellular Score: 0.73
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: -1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.010201
- TAT(Tat/SPI): 0.000437
- LIPO(Sec/SPII): 0.005396
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MLRCLIANRGEIAVRIIRACREYGIETVAVYAKGDEQSLHVHLADQAICIGEANALDSYLNIDRIISAAQITGANAIHPGYGFLSESTKFAQTVEEQGIAFIGPTKKTMEMMGDKITARQTVHHAGVPVIPGSNGAVNHVSEIENLAKDIGYPVVIKAASGGGGKGIRIVKKAEDLEKAFKEAKSEGKKYFDDDRVYVEAFIPVAKHVEVQVMGDGQDNYVHLGERDCSVQRKNQKLIEESPCAALTEERRQQICNDAVKVARAANYRSAGTIEFLVTDTAHYFIEMNARIQVEHTVTEMRAERDLVAAQLYLLEHNHLPFSQSDIQFNGHVIEARINAENPEKKFQPTPGKVTALHLPQGFNVRVDSLLYHGYQVSPYYDSLVAKVIVKSHDRASAIDKLKVTLDEMVIDGFSTTADFLYAVLNYPLYRDGDAKDVDIKFLEKHQIVKGVEL
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 27 [4]
- interaction partners:
SACOL1494 (asnC) asparaginyl-tRNA synthetase [5] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [5] (data from MRSA252) SACOL1016 (fabI) enoyl-ACP reductase [5] (data from MRSA252) SACOL1199 (ftsZ) cell division protein FtsZ [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [5] (data from MRSA252) SACOL1961 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [5] (data from MRSA252) SACOL1960 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [5] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0018 (purA) adenylosuccinate synthetase [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2227 (rplE) 50S ribosomal protein L5 [5] (data from MRSA252) SACOL0585 (rplJ) 50S ribosomal protein L10 [5] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [5] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [5] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: CcpA regulon
CcpA (TF) important in Carbon catabolism; RegPrecise transcription unit transferred from N315 data RegPrecise
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
PLoS One: 2009, 4(12);e8176
[PubMed:19997597] [WorldCat.org] [DOI] (I e) - ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
J Proteome Res: 2011, 10(4);1657-66
[PubMed:21323324] [WorldCat.org] [DOI] (I p) - ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
The Staphylococcus aureus proteome.
Int J Med Microbiol: 2014, 304(2);110-20
[PubMed:24439828] [WorldCat.org] [DOI] (I p) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p)