PRIA_MYCTU
ID PRIA_MYCTU Reviewed; 655 AA.
AC P9WMQ9; L0T6J5; P0A5A5; P71670;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Probable primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000255|HAMAP-Rule:MF_00983}; OrderedLocusNames=Rv1402;
GN ORFNames=MTCY21B4.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. {ECO:0000255|HAMAP-
CC Rule:MF_00983}.
CC -!- SUBUNIT: Component of the primosome. {ECO:0000255|HAMAP-Rule:MF_00983}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00983}.
CC -!- CAUTION: Compared to other bacterial PriA, it has a very divergent
CC helicase domain. {ECO:0000305}.
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DR EMBL; AL123456; CCP44161.1; -; Genomic_DNA.
DR PIR; G70900; G70900.
DR RefSeq; NP_215918.1; NC_000962.3.
DR RefSeq; WP_003407285.1; NZ_NVQJ01000038.1.
DR AlphaFoldDB; P9WMQ9; -.
DR SMR; P9WMQ9; -.
DR STRING; 83332.Rv1402; -.
DR PaxDb; P9WMQ9; -.
DR DNASU; 886716; -.
DR GeneID; 45425380; -.
DR GeneID; 886716; -.
DR KEGG; mtu:Rv1402; -.
DR TubercuList; Rv1402; -.
DR eggNOG; COG1198; Bacteria.
DR OMA; CTVEAAQ; -.
DR PhylomeDB; P9WMQ9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR Gene3D; 3.40.1440.60; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR Pfam; PF17764; PriA_3primeBD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Primosome; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..655
FT /note="Probable primosomal protein N'"
FT /id="PRO_0000102129"
FT ZN_FING 368..380
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 396..411
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 655 AA; 69839 MW; 2C0D0DAD28867E10 CRC64;
MLSVPHLDRD FDYLVPAEHS DDAQPGVRVR VRFHGRLVDG FVLERRSDSD HHGKLGWLDR
VVSPEPVLTT EIRRLVDAVA ARYAGTRQDV LRLAVPARHA RVEREITTAP GRPVVAPVDP
SGWAAYGRGR QFLAALADSR AARAVWQALP GELWADRFAE AAAQTVRAGR TVLAIVPDQR
DLDTLWQAAT ALVDEHSVVA LSAGLGPEAR YRRWLAALRG SARLVIGTRS AVFAPLSELG
LVMVWADADD SLAEPRAPYP HAREVAMLRA HQARCAALIG GYARTAEAHA LVRSGWAHDV
VAPRPEVRAR SPRVVALDDS GYDDARDPAA RTARLPSIAL RAARSALQSG APVLVQVPRR
GYIPSLACGR CRAIARCRSC TGPLSLQGAG SPGAVCRWCG RVDPTLRCVR CGSDVVRAVV
VGARRTAEEL GRAFPGTAVI TSAGDTLVPQ LDAGPALVVA TPGAEPRAPG GYGAALLLDS
WALLGRQDLR AAEDALWRWM TAAALVRPRG AGGVVTVVAE SSIPTVQSLI RWDPVGHAEA
ELAARTEVGL PPSVHIAALD GPAGTVTALL EAARLPDPDR LQADLLGPVD LPPGVRRPAG
IPADAPVIRM LLRVCREQGL ELAASLRRGI GVLSARQTRQ TRSLVRVQID PLHIG
