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Database: UniProt
Entry: A0A0R2F541_9LACO
LinkDB: A0A0R2F541_9LACO
Original site: A0A0R2F541_9LACO 
ID   A0A0R2F541_9LACO        Unreviewed;       752 AA.
AC   A0A0R2F541;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   ORFNames=FC75_GL001422 {ECO:0000313|EMBL:KRN23567.1};
OS   Lacticaseibacillus camelliae DSM 22697 = JCM 13995.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN23567.1, ECO:0000313|Proteomes:UP000050865};
RN   [1] {ECO:0000313|EMBL:KRN23567.1, ECO:0000313|Proteomes:UP000050865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN23567.1,
RC   ECO:0000313|Proteomes:UP000050865};
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:KRN23567.1}.
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DR   EMBL; AYZJ01000027; KRN23567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2F541; -.
DR   STRING; 1423730.FC75_GL001422; -.
DR   PATRIC; fig|1423730.4.peg.1494; -.
DR   Proteomes; UP000050865; 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:UP000050865}.
FT   DOMAIN          7..287
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          288..567
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   752 AA;  84985 MW;  0321BF4425922F9C CRC64;
     MANALLKGMN DKQSEAVLAT EGPLLIMAGA GSGKTRVLTH RVAYLIEEKG INPWRILAIT
     FTNKAAREMK ERIAKMLDPE LAKDVWVSTF HALCVRILRR DIQKLGMNRA FTIADPAEQK
     TLVKHILADL NIDPKRYDPK ALLAAISNAK NDLKTPEQYA KSAGTPFEQT TATVYAEYQK
     RMRSDQALDF DDLIMQTIIL FQKDPETLKF YQNKFQYIHV DEYQDTNEAQ YQLVHMLADG
     YRNLCVVGDA DQSIYGWRGA NMQNILDFKK DYPDAQVVLL EQNYRSTKNI LQAANDVIKN
     NKKRQVKTLW TENKTGDKIT YYRAQSELDE AYFVIKTIEQ DIRVGKRKYG DFAVLYRTNA
     QSRAIEEAFV KSNIPYKMVG GHKFYDRKEI RDALAYFRLV INPDDDMSFN RIVNEPKRGI
     GDTSMEKLQA FATQNGWSLL EAAQNAELSD VSGKARGALA KFGSTIKQIQ AKKDKGTVTD
     LMQAILDDTG YLPTLKNAGT VEADTRIENL QELLSVTQQF DERYEPEDEN SDIFVDFIAD
     LALVSDQDEV EEDAQEVTLM TLHAAKGLEF PVVFLVGMEE GLFPLSRSAM DEKEMEEERR
     LAYVGITRAK SKLYLSNAYA RMLYGQRQNN PQSRFIDEIE PELLETVGQQ APKSSYPFDR
     EANRTARAVT PTYSRHPQGT RAKVVDNAGA PTSTAGKVTW TVGDKAEHRK WGIGTIVKVS
     GKGDDQELDI AFPDMGVKRL LAAFAPITKH VD
//
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