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Database: UniProt
Entry: B1VWF5_STRGG
LinkDB: B1VWF5_STRGG
Original site: B1VWF5_STRGG 
ID   B1VWF5_STRGG            Unreviewed;       517 AA.
AC   B1VWF5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative hydrolase {ECO:0000313|EMBL:BAG18281.1};
GN   OrderedLocusNames=SGR_1452 {ECO:0000313|EMBL:BAG18281.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18281.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG18281.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; AP009493; BAG18281.1; -; Genomic_DNA.
DR   RefSeq; WP_012378543.1; NC_010572.1.
DR   AlphaFoldDB; B1VWF5; -.
DR   GeneID; 6211347; -.
DR   KEGG; sgr:SGR_1452; -.
DR   PATRIC; fig|455632.4.peg.1466; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_013364_3_2_11; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAG18281.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..517
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002771525"
FT   DOMAIN          96..275
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          389..488
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          490..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  56036 MW;  DCDBA0E0C8B6091E CRC64;
     MLLRRRWTSK IALGVAALLT PTLLGTTAAA APAAGPSATA PAASSLSWQG CGGDIPATVQ
     CATLEVPLDH RRPGGRKIDV ALSRIKAAAP AERRGVLIFN PGGPSGSGIF YPLALSGLLP
     QSVKDRYDLI GFDPRGVGAS SPLACGTTTA DERLTYRPYT EATFAQDVAW ARDIADRCRN
     RNKETLRHIT TRNTARDMDI VRAALGERRI SYFGLSYGTY LGSVYTQLFP QRVDRFVLDS
     AVDPKRVWRG MGQSWAEQAE PAFDRWTEWT ARHAARYGLG DTSAEVERLF WDIVARADRE
     PLDLGGTRFD GAEVREYIRW EITHPSVAAR TLGLLRDAAA GKPVPPFPTF VPTDNELASY
     LAIVCGDTRW PTDPAVYRAD SRRDSVRYPL YGDSVSNIFP CAYWDRPVEP ATKIDNKVPA
     LIVQNAWDSQ TPLAAALGLR RALKGSRLVT VDEGQGHGVY ALGISACADD VATRYLTTGR
     LPARDVTCRA DPLPEADSRS ASPGSAAAPA RHPFAGS
//
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