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Database: UniProt
Entry: K2H8Y8_9RHOB
LinkDB: K2H8Y8_9RHOB
Original site: K2H8Y8_9RHOB 
ID   K2H8Y8_9RHOB            Unreviewed;       650 AA.
AC   K2H8Y8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=PSdsA {ECO:0000313|EMBL:EKE43062.1};
GN   ORFNames=OCGS_2653 {ECO:0000313|EMBL:EKE43062.1};
OS   Oceaniovalibus guishaninsula JLT2003.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceaniovalibus.
OX   NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE43062.1, ECO:0000313|Proteomes:UP000006765};
RN   [1] {ECO:0000313|EMBL:EKE43062.1, ECO:0000313|Proteomes:UP000006765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2003 {ECO:0000313|EMBL:EKE43062.1,
RC   ECO:0000313|Proteomes:UP000006765};
RX   PubMed=23144420; DOI=10.1128/JB.01874-12;
RA   Tang K., Liu K., Jiao N.;
RT   "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL   J. Bacteriol. 194:6683-6683(2012).
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC       sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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:EKE43062.1}.
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DR   EMBL; AMGO01000068; EKE43062.1; -; Genomic_DNA.
DR   RefSeq; WP_007427805.1; NZ_AMGO01000068.1.
DR   AlphaFoldDB; K2H8Y8; -.
DR   STRING; 1231392.OCGS_2653; -.
DR   PATRIC; fig|1231392.3.peg.2670; -.
DR   eggNOG; COG2015; Bacteria.
DR   OrthoDB; 7253658at2; -.
DR   Proteomes; UP000006765; Unassembled WGS sequence.
DR   GO; GO:0018741; F:linear primary-alkylsulfatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0018909; P:dodecyl sulfate metabolic process; IEA:InterPro.
DR   CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR   Gene3D; 1.25.40.880; Alkyl sulfatase, dimerisation domain; 1.
DR   Gene3D; 3.60.15.30; Metallo-beta-lactamase domain; 1.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR   InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR   InterPro; IPR029229; Alkyl_sulf_C.
DR   InterPro; IPR029228; Alkyl_sulf_dimr.
DR   InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   PANTHER; PTHR43223; ALKYL/ARYL-SULFATASE; 1.
DR   PANTHER; PTHR43223:SF1; ALKYL_ARYL-SULFATASE BDS1; 1.
DR   Pfam; PF14864; Alkyl_sulf_C; 1.
DR   Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006765};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..650
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003858239"
FT   DOMAIN          121..343
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   650 AA;  71393 MW;  F9FF04303E747AC5 CRC64;
     MRQTYRAMLL ACAMAVPVVP ATAQEASEST KAANRAVLDA LPFDDRTDFE DAERGFIAPL
     PGGSIADADG RTVWDVEAMD FLQGDAPDTA NPSLWRQGKL NHITGLFEVT DGIYQVRNFD
     LSVMSFIRGD SGWIVVDPLI STQTAAAGWA LLREKVADLP VSAVILTHSH ADHFGGIKGI
     VTPEEVAARD IPVIAPEGFV EEAIGENLIA GNAMSRRASY MFGNLLPKGP EGMIGSGLGT
     TTSSGTITLI EPTIVIADTP TEMEVDGVEM VFLNTPGAEA PSEFMFWLPA HKALMQAEII
     NHVLHNLYTL RGTKVRSGDL WAKYIHDVIG RYGDAVEVSF GSHHWPTWGN AEIVEFWEKH
     RDTYRYIHDE TLRLANKGLT MLEIAEEIAL PESLATEFAN RGYYGTVSHN AKAQYQLYFG
     WFSGNPAELH ELPPAEEGAA FVRYAGGADA VIDKARADHD AGNYRWAATA LNHLVFADSE
     NTEARELLAD VYTQLGYQAE SGPWRNFYLT GAQELRQGVT RGATAQTASA DIIRSVPIEM
     YLDYLAMRLD HPRAADADIA LNFVMPDVDE TFAVEVANGV MNYRMDVQED DAQATVTLDR
     ATLDRINLQQ TTFPDAIAAG DVTIEGDRDR LMAFLGLLDD FEFWFDIVTD
//
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