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Database: UniProt
Entry: A0A0R2HXS7_CARDV
LinkDB: A0A0R2HXS7_CARDV
Original site: A0A0R2HXS7_CARDV 
ID   A0A0R2HXS7_CARDV        Unreviewed;       741 AA.
AC   A0A0R2HXS7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   ORFNames=IV74_GL000383 {ECO:0000313|EMBL:KRN57400.1};
OS   Carnobacterium divergens DSM 20623.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN57400.1, ECO:0000313|Proteomes:UP000051658};
RN   [1] {ECO:0000313|EMBL:KRN57400.1, ECO:0000313|Proteomes:UP000051658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN57400.1,
RC   ECO:0000313|Proteomes:UP000051658};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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,
CC         ECO:0000256|RuleBase:RU364053};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRN57400.1}.
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DR   EMBL; JQBS01000007; KRN57400.1; -; Genomic_DNA.
DR   RefSeq; WP_034570878.1; NZ_JQLO01000001.1.
DR   AlphaFoldDB; A0A0R2HXS7; -.
DR   GeneID; 56818146; -.
DR   PATRIC; fig|1449336.4.peg.390; -.
DR   eggNOG; COG0210; Bacteria.
DR   Proteomes; UP000051658; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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   NCBIfam; TIGR01073; pcrA; 1.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000051658}.
FT   DOMAIN          9..288
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          289..565
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   741 AA;  84327 MW;  CA607D3190068DF3 CRC64;
     MVLRDDLLNG MNPRQKEAVI HTEGPLLIMA GAGSGKTRVL THRIAYLIEE KQVNPWNILA
     ITFTNKAAKE MKERVARLMK TGGNDVWVST FHSMCVRMLR RDIDKIGYNK AFTISDPSEQ
     QTLMKRILKE RNIDPKKYDP RAILSQISNA KNELMTPNDY RETASSPFEK IVADCYDDYQ
     KELRRNQAVD FDDLIMLTIR LFQDSPETLD YYQNKFHYIH VDEYQDTNHA QYTLVNLLAK
     RFKNLCVVGD ADQSIYGWRG ANMENILNFE KDYADAEVVL LEQNYRSTKM ILKAANDVIG
     NNSNRKKKKL WTDNDDGEKI TYYRGQSEHD ESRYIVSKMQ EEMRERGLAY GDFAVLYRTN
     AQSRVIEENL LKSNIPYKMV GGHKFYDRKE IRDVLAYLRL IANPEDNMSF ERVVNVPKRG
     IGPGTVDKLR TASNQYGWSM LETALNVSIT PIAGKAAGEL EAFGFMMKDL RQMQEYLPVT
     ELVEEVLKRS GYLKALKAEQ TLESETRIEN IQEFLSVTQQ FEKDSSEDKS LLTFLTDLAL
     VSDLDNLEEE QTSEVTLMTL HAAKGLEFPI VFLIGVEEGV FPLSRALMEE NELEEERRLA
     YVGITRAEQK LYITNAYSRM LYGRTQANAA SRFIAEISEE ALESGNQFTG NTPFRSSGSP
     VSRMQATKAT SSIYQSPVSS KTESGAEKLG WSVGDKALHK KWGTGTVVKV SGDANNLELD
     IAFPEQGIKR LLAAFAPIEK A
//
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