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Database: UniProt
Entry: A0A0A8JMZ8_BACSX
LinkDB: A0A0A8JMZ8_BACSX
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ID   A0A0A8JMZ8_BACSX        Unreviewed;      1047 AA.
AC   A0A0A8JMZ8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Helicase {ECO:0000313|EMBL:BAQ11114.1};
GN   ORFNames=OXB_2643 {ECO:0000313|EMBL:BAQ11114.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ11114.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAQ11114.1, ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ11114.1,
RC   ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL   Genome Announc. 3:e00025-15(2015).
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DR   EMBL; AP013294; BAQ11114.1; -; Genomic_DNA.
DR   RefSeq; WP_041074941.1; NZ_AP013294.1.
DR   AlphaFoldDB; A0A0A8JMZ8; -.
DR   STRING; 98228.OXB_2643; -.
DR   REBASE; 100999; BspOxB1ORF2643P.
DR   KEGG; baco:OXB_2643; -.
DR   HOGENOM; CLU_005588_1_1_9; -.
DR   OrthoDB; 9802848at2; -.
DR   Proteomes; UP000031651; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd09203; PLDc_N_DEXD_b1; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR021835; DUF3427.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR47962; ATP-DEPENDENT HELICASE LHR-RELATED-RELATED; 1.
DR   PANTHER; PTHR47962:SF7; MITOCHONDRIAL ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   Pfam; PF11907; DUF3427; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:BAQ11114.1};
KW   Helicase {ECO:0000313|EMBL:BAQ11114.1};
KW   Hydrolase {ECO:0000313|EMBL:BAQ11114.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:BAQ11114.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031651}.
FT   DOMAIN          221..252
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          337..492
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          551..700
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1047 AA;  120747 MW;  9B09673DCBCE50FC CRC64;
     MQEGIYEQVL NEKIKKSLAS LSGDEYAIEY EKMDVAEAKT MLSSYVSSVT KTALSYVREN
     NKGNEGQALL KQIQTCNEII HVLNRTIDSD DFALLRLDEH AEILTSVYKT INTAHSLKKR
     RVPRPVTPLS QSSLFTGSPT EPNMLEELKK EIITADKIEW LVSFIKWSGI RILIEELREF
     TERGGQLNIL TTSYMEATDY KALEELSKLP NTEIRISLDK ERTRMHAKAY LFKRKTEFST
     AYIGSSNLSN PALTSGLEWN LKVTEKDSFD IIRKFEATFE SYWNDEEFKS LSSENEENWS
     LVRRSLVDRV AESNETYLFD IRPYHYQQEI LDELEAERTL YGHTKNLVVA ATGVGKTVIS
     AFDFKRYLQE NPNAKLLFIA HREEILKQSM HTFRAILKDA NFGEMFVGRH EPTSFDHLFM
     SIQSWNSREM INKTTADFYD FVIVDEFHHA TAPTYRALLE YYKPAILLGL TATPERMDNE
     NVLGYFDDRI ASEMRLTEAI DRKLLSPFHY FCVTDTVDLS AIKWSKKGYD VEALSNVYTS
     NDRRSDLVIQ SIKKYVTSLE QVKGLGFCVS VEHAKYMAAY FNQKNIASIA LHGNSSVEDR
     ETAKRKLVAG EITFIFVVDL YNEGIDIPEV NTVLFLRPTE SLTVFLQQLG RGLRLAEGKE
     CLTVLDFVGQ AHVDYPFEEK FRALMGRTKH SVRHYLENGF FHLPKGSVIQ MEKQAKEYIL
     RNVKEVKNSK QNLIKMMKHF EQDTGEPLTL VNFLQFYHLS LAEFYGRGKN RSFERLKVEA
     GIGNHFESEF EEVVTKRIHA LFHLDSPDLI RFYQTYLAKG IIENEEQRLM IGMFYYSFFD
     APPEDFGFTS IHEGIQMLLA TEALKSEVRQ VLDACMETIR TVKKPSPFEF ISPLRVHAQY
     TSDQVLAAFG YFNEAAKPAF REGVKYFEDK QTDVFFITLN KSDKDFSPST LYEDYAISDR
     LFHWQSQNKT SDTSPTGKRY INQRQTGNKI ALFVRESKQK DGYTSPFTFL GTADYVSHEG
     NRPISFVWRL HESIPAKLMP VANKSVL
//
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