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Database: UniProt
Entry: Q6LM49_PHOPR
LinkDB: Q6LM49_PHOPR
Original site: Q6LM49_PHOPR 
ID   Q6LM49_PHOPR            Unreviewed;       465 AA.
AC   Q6LM49;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   Name=C5026 {ECO:0000313|EMBL:CAG21629.1};
GN   OrderedLocusNames=PBPRA3331 {ECO:0000313|EMBL:CAG21629.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21629.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity and contains
CC       distinct active sites for ATP binding, DNA binding, and interaction
CC       with DnaC protein, primase, and other prepriming proteins.
CC       {ECO:0000256|ARBA:ARBA00003574, ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; CR378673; CAG21629.1; -; Genomic_DNA.
DR   RefSeq; WP_011219877.1; NC_006370.1.
DR   AlphaFoldDB; Q6LM49; -.
DR   STRING; 298386.PBPRA3331; -.
DR   KEGG; ppr:PBPRA3331; -.
DR   eggNOG; COG0305; Bacteria.
DR   HOGENOM; CLU_005373_0_0_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT   DOMAIN          194..461
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   465 AA;  51762 MW;  580DC8D5F997EFDC CRC64;
     MADNSKPKKY KDTQMDAIKM PPHSLEAEQS VLGGLMLDNE KWDRVAEKVV SKDFYSRPHR
     IIFEATAALL EGGQPLDLIT LSEHLERADK LEDVGGFAYL AELAKNTPSA ANIGAYAEIV
     RERALIRDMI AVANDIADAG YDPQGRTSED LLDMAESKVF AIAEQRTNDN EGPQSVDIIL
     EKTLERIELL YQSPQDGVTG VSTGFSDLNK KTAGLQGSDL IIVAARPSMG KTTFAMNLCE
     NAAMDQEKPV LIFSLEMPAE QIMMRMLASL SRVDQTKIRT GQLDDEDWAR ISSTMGILME
     KKNMFIDDSS SLTPTELRSR ARRIARDHGG LSMIMIDYLQ LMRVPGMQDN RTLEISEISR
     SLKALAKELN VPVVALSQLN RSLEQRADKR PINSDLRESG AIEQDADLIM FIYRDEVYNE
     ESALKGIAEI IIGKQRNGPI GSVRLTFQGQ YSRFDNYAGP AFDDE
//
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