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Database: UniProt
Entry: C5ZXI3_9HELI
LinkDB: C5ZXI3_9HELI
Original site: C5ZXI3_9HELI 
ID   C5ZXI3_9HELI            Unreviewed;       702 AA.
AC   C5ZXI3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:EES89851.1};
GN   ORFNames=HCAN_1140 {ECO:0000313|EMBL:EES89851.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89851.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES89851.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(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};
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}.
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DR   EMBL; CM000776; EES89851.1; -; Genomic_DNA.
DR   RefSeq; WP_006655846.1; NZ_DS990368.1.
DR   AlphaFoldDB; C5ZXI3; -.
DR   STRING; 537970.HCAN_1140; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_7; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000007032; Chromosome.
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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; 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; 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   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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.
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};
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:UP000007032}.
FT   DOMAIN          7..281
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          282..561
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   702 AA;  80722 MW;  D2ACFA477473BAA5 CRC64;
     MQEKFLNQLN TSQKQAVTTI EGALLILAGA GSGKTKTITT RLAYLIDEVG IPPSNTLTLT
     FTNKAANEMQ KRALNMLKKS TSHPPLLCTF HKFGLLFLKF YISLLGRKIN FILADSDDTK
     KILKELNCDL APLPLIISEI SRYKNSQITP QEALKNAHNE LYKHIAKVYL NYQETLLQNN
     MVDFDDLLLL PIEILKSNPN VATEISQKYQ YIMVDEYQDT NDLQYQLLKY LCTTHNNICV
     VGDDDQSIYS WRGANIQNIL NFSQHFKGAK TIKLEENYRS SKSILNAANH LISNNKERLG
     KTLKSTLDEG KPIEVLHSYD EQEEAKNLSK IIKKLLQNGI NPKDIAILFR LNALSRSLEE
     GFNRERIPYV LVGTIRFYER SEIKDVISYF RVLTNINDDF SLLRIINKPK RGIGKTTLEK
     LKSLSQIHHC SIYELFSNQS PQLLQQEISK KTYNTIWEFF KTIKELQDLQ AQSSLKFLDD
     FEEKIGLCKA LSQNSEEVDR VSNIEEFYGL YREYVKQNPL MELEDFLNEL ALRSDQEDTE
     LRNEQKGVEG VSCMSVHSSK GLEFDYVFII GLEEGFFPMA REDTNLQEER RLGYVAFTRA
     KKELYLSYVD SRFYRGNRTS LYPSRFLAES KILAKENFLN QNTTDISKTA YEIGFQRGDC
     VMHKIFGAGR ITEITKSGQE IKLKINFGGL LREILSGYVT KV
//
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