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Database: UniProt
Entry: A0A0J6HLG7_9BACI
LinkDB: A0A0J6HLG7_9BACI
Original site: A0A0J6HLG7_9BACI 
ID   A0A0J6HLG7_9BACI        Unreviewed;       790 AA.
AC   A0A0J6HLG7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   ORFNames=AB447_212685 {ECO:0000313|EMBL:KRT95439.1}, COP00_08175
GN   {ECO:0000313|EMBL:ATH95459.1};
OS   Bacillus glycinifermentans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT95439.1, ECO:0000313|Proteomes:UP000036168};
RN   [1] {ECO:0000313|EMBL:KRT95439.1, ECO:0000313|Proteomes:UP000036168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GO-13 {ECO:0000313|EMBL:KRT95439.1,
RC   ECO:0000313|Proteomes:UP000036168};
RX   PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA   Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT   "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT   paste.";
RL   Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN   [2] {ECO:0000313|EMBL:KRT95439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GO-13 {ECO:0000313|EMBL:KRT95439.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ATH95459.1, ECO:0000313|Proteomes:UP000218414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH95459.1,
RC   ECO:0000313|Proteomes:UP000218414};
RA   Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT   "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; CP023481; ATH95459.1; -; Genomic_DNA.
DR   EMBL; LECW02000004; KRT95439.1; -; Genomic_DNA.
DR   RefSeq; WP_048406433.1; NZ_LECW02000004.1.
DR   AlphaFoldDB; A0A0J6HLG7; -.
DR   STRING; 1664069.BGLY_3199; -.
DR   PATRIC; fig|1664069.3.peg.2561; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000036168; Unassembled WGS sequence.
DR   Proteomes; UP000218414; Chromosome.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ATH95459.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}.
FT   DOMAIN          151..241
FT                   /note="RecD helicase-like helix-hairpin-helix"
FT                   /evidence="ECO:0000259|Pfam:PF14490"
FT   DOMAIN          586..654
FT                   /note="RecD-like DNA helicase SH3"
FT                   /evidence="ECO:0000259|Pfam:PF18335"
FT   DOMAIN          673..721
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   BINDING         362..366
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   790 AA;  88912 MW;  C52E91DC2686B21D CRC64;
     MQMDEASFLK GTVTTVIYHN ETNLYTVLKV KVQETSESFD EKTVSVTGYF PAIFEDETYT
     FYGKKASHPK FGLQFQTDHF KKEVPTTKEG VIQYLSSDLF EGIGKKTAEE IVNKLGEGAI
     NRILGDASVL YDVPKLSKKK ADKLAAALQQ HQGLEQIMIS LSEFGFGPQL SMKIYQAYES
     ETLDKIRENP YQLVKDVEGI GFVKADELGG RMGISGRHPE RVKAAILFTI EAACLQEGHT
     YIETKQLIIE TQKLLNQSSG EEKVTEMDVA DSIISLGEQK ELFIEDDRCY YPSLYYAEQS
     FAKRVLTIAE QTEYDDQFPE SEFLLALGEL EERMQVQYAP SQKEAIQKAL MSPMLLLTGG
     PGTGKTTVIR GIVELYSELH GLSLNPADYK KDEAFPFVLA APTGRAAKRM SESTGLPAVT
     IHRLLGWNGS EGFTHDEDNP IEGRLVIIDE TSMLDIWLAN QLFKAIPNRI QVIMVGDEDQ
     LPSVGPGQVL RDLLASNVIA SVRLTDIYRQ AEGSSIVELA HDMKKGRLPQ NLTAPTKDRS
     FIRCRQQQMK EVVEKVVQNA LQKGYSARDI QVLAPMYRGP AGINELNALL QNILNPPKQK
     GRELKYGDVV YRTGDKVLQL VNQPEHNVFN GDMGEIVSIF YAKENTEKED MAVVSFDGNE
     ITFTKKDFNQ FTHAYCCSIH KSQGSEFPIV ILPVVKSYYR MLRRNLLYTA ITRSKKFLIL
     CGEEEALQWG IKNKDSSERQ TSLKRRLQQA AHEEDEELAA LQKELPFSVY DANIGMEGIT
     PFDFMEKEAE
//
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