ID A0A0F7FYB1_9ACTN Unreviewed; 536 AA.
AC A0A0F7FYB1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:AKG45140.1};
GN ORFNames=SXIM_37560 {ECO:0000313|EMBL:AKG45140.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45140.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009922; AKG45140.1; -; Genomic_DNA.
DR RefSeq; WP_043178505.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7FYB1; -.
DR STRING; 408015.SXIM_37560; -.
DR KEGG; sxi:SXIM_37560; -.
DR PATRIC; fig|408015.6.peg.3807; -.
DR HOGENOM; CLU_013364_3_1_11; -.
DR Proteomes; UP000034034; 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; 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; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039715109"
FT DOMAIN 431..535
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 20..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 56661 MW; 430F41D1183443F6 CRC64;
MMRVRLAAVL TTLAVLPAAG CSAGGSPERV ADTTTPPPSG SPVPTDSLPD SLTAQKLEWS
ECKTPDSSQG DSGGSPSPLP DGAPWECATM KAPVNYADPE GDTLDLALIR ARSTGGEGER
IGSLLFNFGG PGGSGVVTLP AFGSDYTELA KRYDLVSFDP RGVGDSDGLV CMSDKQLDDY
FAADPVPSGE AEERDFTNRL RAFDNACEAA AGPLLPHLTT VNTARDMDLM RQVLGDNKLH
YFGISYGTQL GGVYAHLFPQ RVGRAALDAV VDPTADAREG ALAQTKGFQQ ALTTYMESCA
QSENCPLGST PQEGEQKLKD FLENLRSHPL PTQDPDGRPL TESLAWSGIA QSLYSEDFWP
FLTQGLEEAM ASENPDGTIL LTLGDSMNGR NQNGTYSTLQ SSLVAINCAD TDQRYDVADV
HDALPEFTDA SPVFGPGMAW SLLSCTDWPV TGTQSHPDVS TTTDATLLLI GTTGDPATPY
AGTQNMKEAL GKDKAVELTY EGEGHGAYNS GDTCVKDTVN AYLLDGDVPT DGKTCP
//
