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
//