ID A0A3A9H8P4_9FIRM Unreviewed; 741 AA.
AC A0A3A9H8P4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN Name=pcrA {ECO:0000313|EMBL:RKJ66847.1};
GN ORFNames=D7Y06_06845 {ECO:0000313|EMBL:RKJ66847.1};
OS Roseburia sp. 1XD42-69.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=2320088 {ECO:0000313|EMBL:RKJ66847.1, ECO:0000313|Proteomes:UP000279120};
RN [1] {ECO:0000313|EMBL:RKJ66847.1, ECO:0000313|Proteomes:UP000279120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1XD42-69 {ECO:0000313|EMBL:RKJ66847.1,
RC ECO:0000313|Proteomes:UP000279120};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-2018) 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}.
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:RKJ66847.1}.
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DR EMBL; RAZG01000009; RKJ66847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9H8P4; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000279120; 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|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000279120}.
FT DOMAIN 5..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 286..560
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 644..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 741 AA; 83986 MW; B88F26AB7010A6FD CRC64;
MSVYDTLNEP QKEAILKTEG PLLILAGAGS GKTRVLTHRT AYLIEEKGVN PWNILAITFT
NKAAGEMRER ISAMVGHGSE SIWVSTFHSA CVRILRRYID RIGFDTNFTI YDADDQKSLM
KDICKRLQID TKIYKEKTFL AAISSAKDEM IGVEEFTRNA GVDFALQKQA QVYREYQNAL
KKNNALDFDD LILQTVELFR KEEEVLDSYQ ERFRYIMVDE YQDTNTAQFE LIHLLAGKYK
NLCVVGDDDQ SIYKFRGANI YNILNFEKHF PQACVIKLEQ NYRSTQNILD AANHVIANNR
GRKEKRLWTA NGQGEKLVLK QLETSYDEAD FVTRDITEKV YKENYNYRDC AILYRTNAQS
RLFEEKFVVS NIPYKIVGGV NFYARREIKD LLCYLKTIDN ARDDLAVRRI INVPKRGIGA
ASLNKVQIFA DANGMSFYDA LKKAEEIPGL GRAAGKIRPF VTFIQAMRSK LDLIGLTDLL
NEIIETTGYV EELELEGTEE AAGRIENIDE LISKIAAYEE DTQEPTLSGF LEEVALVADI
DSLEEDSNYV VLMTLHSAKG LEFPNVYLAG MEDGLFPSYM SIVSDTAMED LEEERRLAYV
GITRAKEHLV ITSARQRMIR GETQFNRLSR FVQEIPSVLF GQEAAPAPKK STETKNPYRQ
AKDSFKKKPV AVSGLAAAKN FGAAEKKALD YTEGDRVSHI KFGEGIVTNI VEGGRDYEVT
VDFDKAGTKK MFASFAKLKK L
//
