PRIA_BACSU
ID PRIA_BACSU Reviewed; 805 AA.
AC P94461; O34941;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=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}; Synonyms=yloJ;
GN OrderedLocusNames=BSU15710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-805.
RC STRAIN=168;
RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835;
RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.;
RT "A survey of polypeptide deformylase function throughout the eubacterial
RT lineage.";
RL J. Mol. Biol. 266:939-949(1997).
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}.
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DR EMBL; Y13937; CAA74261.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13444.1; -; Genomic_DNA.
DR EMBL; Y10304; CAA71348.1; -; Genomic_DNA.
DR PIR; A69682; A69682.
DR RefSeq; NP_389453.1; NC_000964.3.
DR RefSeq; WP_003232079.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P94461; -.
DR SMR; P94461; -.
DR IntAct; P94461; 1.
DR STRING; 224308.BSU15710; -.
DR PaxDb; P94461; -.
DR PRIDE; P94461; -.
DR EnsemblBacteria; CAB13444; CAB13444; BSU_15710.
DR GeneID; 938122; -.
DR KEGG; bsu:BSU15710; -.
DR PATRIC; fig|224308.179.peg.1711; -.
DR eggNOG; COG1198; Bacteria.
DR InParanoid; P94461; -.
DR OMA; RCHYCGY; -.
DR PhylomeDB; P94461; -.
DR BioCyc; BSUB:BSU15710-MON; -.
DR Proteomes; UP000001570; Chromosome.
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; -; 2.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00595; priA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Primosome; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..805
FT /note="Primosomal protein N'"
FT /id="PRO_0000102116"
FT DOMAIN 282..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 545..699
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 510..522
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 537..553
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 391..394
FT /note="DEAH box"
FT BINDING 295..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT CONFLICT 232
FT /note="A -> V (in Ref. 3; CAA71348)"
FT /evidence="ECO:0000305"
FT CONFLICT 691..698
FT /note="FYQHEMAH -> VLSSMKWRT (in Ref. 3; CAA71348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 91353 MW; 7E0D2970805AC948 CRC64;
MNFAEVIVDV STKNIDRPFD YKIPDHLKGM IKTGMRVIVP FGPRKIQGFV TAVKEASDLS
GKSVKEVEDL LDLTPVLTEE LMILSSWLSD KTLSFKITAL QAMLPAALKA KYEKELKIAH
GADLPPQVER LFSETKTLLY SDIPDHETLK LIQRHVQKGD IDVTYKVAQK TNKKMVRHIQ
ANASKEELAK QAEGLSRQAA KQQAILHFLI SEPEGVKIPA AELCKKTDTS SATIKTLIQK
GLLKESYEEV YRDPYQDKMF KKTEPLPLTD EQRAAFEPIR ETLDSDEHKV FLLHGVTGSG
KTEIYLQSIE KVLAKGKEAI VLVPEISLTP QMVNRFKGRF GSQVAVMHSG LSTGEKYDEW
RKIHRKEVRL VVGARSAIFA PFENLGMIII DEEHESSYKQ EEMPRYHAKE VAIKRAEHHS
CPVVLGSATP TLESYARAQK GVYELLSLKH RVNHRVMPEV SLVDMREELR NGNRSMFSVE
LMEKLEETIA KGEQAVLFLN KRGYSSFVMC RDCGYVPQCP HCDISMTYHR YGQRLKCHYC
GHEEPVPHTC PECASEHIRF FGTGTQRVEE ELTKVLPSAR VIRMDVDTTS RKGAHEKLLS
AFGEGKADIL LGTQMIAKGL DFPNVTLVGV LSADTTLHIP DFRSAEKTFQ LLTQVSGRAG
RHEKPGHVII QTYTPSHYSI QLTKTHDYET FYQHEMAHRR EQSYPPYYYL ALVTVSHEEV
AKAAVTAEKI AHFLKANCGA DTKILGPSAS PIARIKDRYR YQCVIKYKQE TQLSALLKKI
LEHYKREIEQ KHVMISIDMN PYMMM
