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Database: UniProt
Entry: A0A143Y8L1_9LACT
LinkDB: A0A143Y8L1_9LACT
Original site: A0A143Y8L1_9LACT 
ID   A0A143Y8L1_9LACT        Unreviewed;       759 AA.
AC   A0A143Y8L1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   ORFNames=TR210_375 {ECO:0000313|EMBL:CZQ84613.1};
OS   Trichococcus ilyis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Trichococcus.
OX   NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ84613.1, ECO:0000313|Proteomes:UP000076878};
RN   [1] {ECO:0000313|EMBL:CZQ84613.1, ECO:0000313|Proteomes:UP000076878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ84613.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FJNB01000002; CZQ84613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143Y8L1; -.
DR   STRING; 640938.TR210_375; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000076878; 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: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|PROSITE-ProRule:PRU00560,
KW   ECO:0000256|RuleBase:RU364053};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW   ECO:0000256|RuleBase:RU364053}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
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   REGION          643..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   759 AA;  86290 MW;  B6495F4414A44F36 CRC64;
     MQQKHDLIKG MNPRQAEAVL ATEGPLLIMA GAGSGKTRVL THRMAYLLEE KSVNPWNILA
     ITFTNKAAKE MKERVIRLVG TVGNDMWVST FHSMCVRILR RESEQIGYAR SFTICDQSET
     ETLMKRIIRE KNLDSKKFDH RMILGRISQA KNELQTPKEF SEFAGGYIDN IVYECYKDYQ
     KALENSQSMD FDDLILLTVK LFKEHPETLS YYQNKFHYIH VDEYQDTNYA QYQLVQLLAS
     KFKNICVVGD ADQSIYGWRG ADMENILNFE KDYPDAKVVL LEQNYRSTKK ILRAANDVIQ
     NNVNRKEKEL WTDNPEGDNI VYFRGQSEHD EARYVITKML KEVRENKRQY GDFAVLYRTN
     AQSRVIEENL LKSNIPYKMV GGRKFYDRKE IKDLLAYLRL IVNPADDLSF GRIVNVPKRG
     IGDASVEKLR EFADMHNLTL LQAAHDVALS SVSGKAAKEL KKFATTMDNL QKMQEFLPIT
     ELVQEMLSQT TYLEALEMEK TLESEARIEN INEFLSVTQE FDKTNADNLD LTSFLTDLAL
     VSDLDQIEEE PQSEVTLMTM HAAKGLEFPI VFIIGMEDGI FPSSRAFMDE DQMEEERRLA
     YVGITRAEQK LFLTNAYSRT LYGRSMSNPA SRFLDELDGS VLDREDSSGS TSTPSSFSSR
     PASSGNRWKT ASDTRQEKAF SQPFSAGARE KTTQSVQQTG NSGADRLGWA VGDKASHKKW
     GVGVVVQTSG EGDGLTLDIA FKNIGIKRLL ASFAPIEKA
//
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