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Database: UniProt
Entry: C8WTI7_ALIAD
LinkDB: C8WTI7_ALIAD
Original site: C8WTI7_ALIAD 
ID   C8WTI7_ALIAD            Unreviewed;       756 AA.
AC   C8WTI7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE            EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN   OrderedLocusNames=Aaci_0682 {ECO:0000313|EMBL:ACV57729.1};
OS   Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS   DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS   NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV57729.1, ECO:0000313|Proteomes:UP000001917};
RN   [1] {ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC   15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC   {ECO:0000313|Proteomes:UP000001917};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT   acidocaldarius DSM 446.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV57729.1, ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC   15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC   {ECO:0000313|Proteomes:UP000001917};
RX   PubMed=21304673; DOI=10.4056/sigs.591104;
RA   Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA   Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA   Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA   Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT   (104-IA).";
RL   Stand. Genomic Sci. 2:9-18(2010).
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; CP001727; ACV57729.1; -; Genomic_DNA.
DR   RefSeq; WP_012810088.1; NC_013205.1.
DR   AlphaFoldDB; C8WTI7; -.
DR   STRING; 521098.Aaci_0682; -.
DR   KEGG; aac:Aaci_0682; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_2_9; -.
DR   Proteomes; UP000001917; Chromosome.
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:UP000001917}.
FT   DOMAIN          12..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..575
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   756 AA;  85704 MW;  B6E46B13181947B6 CRC64;
     MVATAGASDI LKGLNEKQRE AVTATDGPVL VIAGAGSGKT SVLTRRIAYL IAERRVPPWA
     ILAITFTNKA AREMEERIER LVGPVASDIW TSTFHAMCAR ILRRDIHHLG YTSAFTVLDA
     ADQVSLVRRL MQEMNIDVRK FEPRAVLHAI SQHKNELRSA EKALDLAGSP YDKMVGDVYL
     AYERRLRENQ ALDFDDLLVK TVELFRKVPD VLAYYQHRFS HIHVDEYQDT NHAQYVLVKL
     LAERRRNLCV VGDSDQSIYG WRGADIRNIL EFQRDYPDAR VIRLEQNYRS TGRILRIANQ
     VIQHNQMRLE KNLWTDRGEG EKAKLFVAPD ERVEADWVAD EIARMVANGR EYRDVAILYR
     TNAQSRVLEE AFLQRGIPYR IYGGLRFYER REVKDVIAYL RLIANPNDDV SFLRVVNVPK
     RGIGDTTLEK LAEYARHRGT SLFEAALHAL EAGISKKAAS ALQSFVELIQ TLQLQRAFLP
     LTDLTDELLD RSGYREALRA ERSLEAENRL ENLDEFLSLT REFDEDGVPD GEMGALEQFL
     THVALVSDAD LPGGRPGRRE DLDEVSMMTL HAAKGLEFPV VFLVGLEEGV FPHRRALDGG
     EELEEERRLC YVGITRAMER LYLTTCRSRM LFGERRSFTP SRFLSEMPAS DIERAGEEDA
     MFGWGWRDAR AGVRAPAHAV ADAASGPRMS VPRSFGADLS VPYEPGDLVE HRKWGRGVIV
     AKSGEGESLE LVVRFEDPIG EKRLFAKFAP IHKVDP
//
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