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Database: UniProt
Entry: A0A0R1GWR9_9LACO
LinkDB: A0A0R1GWR9_9LACO
Original site: A0A0R1GWR9_9LACO 
ID   A0A0R1GWR9_9LACO        Unreviewed;       817 AA.
AC   A0A0R1GWR9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=FC07_GL000243 {ECO:0000313|EMBL:KRK35127.1};
OS   Loigolactobacillus bifermentans DSM 20003.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK35127.1, ECO:0000313|Proteomes:UP000051461};
RN   [1] {ECO:0000313|EMBL:KRK35127.1, ECO:0000313|Proteomes:UP000051461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK35127.1,
RC   ECO:0000313|Proteomes:UP000051461};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
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:KRK35127.1}.
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DR   EMBL; AZDA01000082; KRK35127.1; -; Genomic_DNA.
DR   RefSeq; WP_057904800.1; NZ_AZDA01000082.1.
DR   AlphaFoldDB; A0A0R1GWR9; -.
DR   STRING; 1423726.FC07_GL000243; -.
DR   PATRIC; fig|1423726.3.peg.252; -.
DR   Proteomes; UP000051461; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; IPR003593; AAA+_ATPase.
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; PF13604; AAA_30; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 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};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000051461}.
FT   DOMAIN          356..514
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         367..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   817 AA;  90852 MW;  2922D2CA3DBD82FD CRC64;
     MATEMTLFPE EKAQPEVTGK VSAIFFQNPD NFYKVLLVQV EQVNFDWTDK EVVVTGSFGD
     IKEEESYRFV GKMVTHPKYG MQFQASNYEK DQPTTKAGLI AYLAGDQFPG IGQKTAEKIV
     SALGLDAIQK ILADPAVLKN LGIKTERIQT LVEQLTKNNG MDQIIIGLNS YGFGSQLAYT
     IYEKYHEETL QVLAERPYQL VKDIPGIGFK KADQIAAQQH IAADAPERIQ AAILQEITEL
     TQAEGDTYTQ AQPLLNATLN LLRESRQQAL SPDAVANQMI QLADQGDIIS EDNRIYLRQL
     YRSEWKIAEN LQRLMKMVSL PDYDDAQVDR EIRRIEKLFK MTYGDSQIAT IKAALNSPVF
     LLTGGPGTGK TTIINAIVLL FAKLNDLSLE LTDYKEKPFP ILLAAPTGRA AKRMSEVTGL
     PASTIHRLLG LNGRENGDVI TKDLEGALLI IDEMSMVDTS LFRLLMQAVS NNMQVILVGD
     RDQLPSVGPG QVFSDLLMSH ILPSSELTEI YRQDDGSSII PLAHAIKGGR LPADFTKNQK
     DRSFIPCSAY QVAQAIDQIV TRAKSKGFTS QDIQVLAPMY RGAAGITKLN LEVQQILNPK
     TGPRQKEITF RQQTFRVGDK VLHLVNSPEL NVFNGDIGEI VGVELAKDKG NEDKTDKLTI
     RFDATEVTYG RNDWSKLTLA FCTSIHKAQG SEFKMVILPI VHQYQRMLQR NLLYTAITRA
     QDLLILIGEQ DAFATAVAHE SINRKTTLQQ RLQTVFNGEQ PVQTPAKKEP AETVTATPVV
     AMSEPDQTIL TTAMVEQRQV DPMIGMKNLT PQDFKTA
//
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