Jump to navigation
Jump to search
⊟Summary[edit | edit source]
- pan ID?: SAUPAN003376000
- symbol?: rnhC
- synonym:
- description?: ribonuclease HIII
- ribonuclease HIII
- putative ribonuclease
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 3739984..3740925
- synteny block?: BlockID0024590
- occurrence?: in 100% of 34 strains
rnhC : ribonuclease H-III [1]
Staphylococci produce different paralogues of Ribonuclease H to introduce nicks in different RNA-DNA hybrid structures. The most prevalent RNA-DNA hybrids in bacteria are Okazaki fragments generated during lagging strand synthesis. RNase H-III introduces a nick 5'- to a string of ribonucleotides in a DNA-RNA duplex. The nick allows DNA Pol I access to the ribonucleotides which it removes with its 5'→3' exonuclease activity and then fills in with deoxyribonucleotides. Alternatively, the exonuclease function can be accomplished using the 5'→3' flap riboexonuclease Fen, although DNA polymerase is still required to fill in the new ssDNA region. In bacteria such as E. coli, the RNase H-III activity is performed by RNase H-I. However, in Bacillus subtilis, RNase H-I is catalytically inactive and functionally-replaced with RNase H-III. Staphylococci do encode an RNase H-I orthologue but its catalytic activity is not clear.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1096
08BA02176:
C248_1167
11819-97:
MS7_1096 (rnhC)
6850:
RSAU_001024 (rnhC)
71193:
ST398NM01_1136
ECT-R 2:
ECTR2_994 (rnhC)
ED133:
SAOV_1136c
ED98:
SAAV_1107 (rnhC)
HO 5096 0412:
SAEMRSA15_09700
JH1:
SaurJH1_1221
JH9:
SaurJH9_1199
JKD6008:
SAA6008_01094 (rnhC)
JKD6159:
SAA6159_00994 (rnhC)
JSNZ:
JSNZ_001105 (rnhC)
LGA251:
SARLGA251_10520
M013:
M013TW_1073
MRSA252:
SAR1113
MSHR1132:
SAMSHR1132_09860
MSSA476:
SAS1074
Mu3:
SAHV_1131
Mu50:
SAV1140
MW2:
MW1023
RF122:
SAB1004c
ST398:
SAPIG1136 (rnhC)
T0131:
SAT0131_01182
TCH60:
HMPREF0772_12093 (rnhC)
TW20:
SATW20_11340 (rnhC)
USA300_TCH1516:
USA300HOU_1075 (rnhC)
VC40:
SAVC_04865
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
N315 MANIVFKLSDKDITTLMSRITFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
NCTC8325 MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
Newman MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
USA300_FPR3757 MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
********************:***************************************
COL SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
N315 SKELLPQHSQLNTNKTKKKNMANSSLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
NCTC8325 SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
Newman SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
USA300_FPR3757 SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
*:********************** ***********************************
COL KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
N315 KEHVPILKTLGVDDSKKLTDTKIVELAEQLVAFIPHSLLTLHNDKYNIQQAKGWTQVKMK
NCTC8325 KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
Newman KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
USA300_FPR3757 KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
*******************************:***********:****************
COL AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
N315 AVLHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
NCTC8325 AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
Newman AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
USA300_FPR3757 AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
*.**********************************************************
COL IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
N315 IAVASIISRYAFITYMDQISKYINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
NCTC8325 IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
Newman IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
USA300_FPR3757 IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
************:******** **************************************
COL NREKAQKILKPL
N315 NREKAQKILKPL
NCTC8325 NREKAQKILKPL
Newman NREKAQKILKPL
USA300_FPR3757 NREKAQKILKPL
************
- ↑ Scott A Reiling, Kohei Homma, Oluwatoyin A Asojo
Purification and crystallization of RNase HIII from Staphylococcus aureus.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2011, 67(Pt 1);79-82
[PubMed:21206030] [WorldCat.org] [DOI] (I p)Justin R Randall, William G Hirst, Lyle A Simmons
Substrate Specificity for Bacterial RNases HII and HIII Is Influenced by Metal Availability.
J Bacteriol: 2018, 200(4);
[PubMed:29084857] [WorldCat.org] [DOI] (I e)Justin R Randall, Taylor M Nye, Katherine J Wozniak, Lyle A Simmons
RNase HIII Is Important for Okazaki Fragment Processing in Bacillus subtilis.
J Bacteriol: 2019, 201(7);
[PubMed:30670546] [WorldCat.org] [DOI] (I e)Anna Lipońska, Mee-Ngan F Yap
Hibernation-Promoting Factor Sequesters Staphylococcus aureus Ribosomes to Antagonize RNase R-Mediated Nucleolytic Degradation.
mBio: 2021, 12(4);e0033421
[PubMed:34253058] [WorldCat.org] [DOI] (I p)