⊟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]
⊟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)