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Database: UniProt
Entry: C0Q692_SALPC
LinkDB: C0Q692_SALPC
Original site: C0Q692_SALPC 
ID   C0Q692_SALPC            Unreviewed;       503 AA.
AC   C0Q692;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=SPC_4469 {ECO:0000313|EMBL:ACN48522.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN48522.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN48522.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN48522.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR   EMBL; CP000857; ACN48522.1; -; Genomic_DNA.
DR   RefSeq; WP_001120833.1; NC_012125.1.
DR   AlphaFoldDB; C0Q692; -.
DR   KEGG; sei:SPC_4469; -.
DR   HOGENOM; CLU_023291_2_0_6; -.
DR   Proteomes; UP000001599; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF30; F-BOX DNA HELICASE 1; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ACN48522.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          179..230
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00580"
FT   DOMAIN          357..458
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13361"
FT   REGION          474..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  57379 MW;  CDA181C257B61D06 CRC64;
     MPHTDTPEQA AVIAWKGERL VVCAFAGSGK TTTLRRYAEE NPTERMLYIA YNRAIRDEAE
     QKFPFNVTCK TSHQLAWPTV GKHYSHRLIN SLRLTYVARA LNSRNWLLAR LTLDVLNRFI
     CSAATDITPE HMPDPDDCKG LQPGQILFSA KKIWAMMSAR QGDFPVTHDT YLKLYQLSKP
     NLSSRYTTLL FDEAQDANPV ISAIVLNQTC RVVLVGDTHQ QIYRFRGADN AMQAPQLENS
     DRLWLTHSFR FGPEVAGVAN RLLALKGETH QITGKGGAGR VLLTMPRNFG HHAVLHRSVC
     GVIRTALHWS LAGRKVFWVG GMESYRIEDL LDLYWFSIDM SERMRHDRLT REYRDYDEYL
     QIAEDTGDVE MKQGIFILEQ FFPLPDRLNT LREQRVISES EADVTVCTAH RSKGLEWDRV
     KLHDDFLDIL DPDMPESQRQ DEINLMYVAA TRARKVLITD PILHELLIQP RAEDIAGTSA
     DKSGESEVST ENDKKGTEYV PES
//
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