ID A0A2T6E384_9GAMM Unreviewed; 445 AA.
AC A0A2T6E384;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:PTY35832.1};
GN ORFNames=BGP77_00430 {ECO:0000313|EMBL:PTY35832.1};
OS Saccharospirillum sp. MSK14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Saccharospirillum.
OX NCBI_TaxID=1897632 {ECO:0000313|EMBL:PTY35832.1, ECO:0000313|Proteomes:UP000244044};
RN [1] {ECO:0000313|EMBL:PTY35832.1, ECO:0000313|Proteomes:UP000244044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK14-1 {ECO:0000313|EMBL:PTY35832.1,
RC ECO:0000313|Proteomes:UP000244044};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Saccharospirillum sp. MSK14-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:PTY35832.1}.
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DR EMBL; MIES01000033; PTY35832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6E384; -.
DR Proteomes; UP000244044; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000244044};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 99..168
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 398..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48250 MW; 2A3A19E7C2882023 CRC64;
MPSNTDAKGT LMKLIRSPWL TAMTALIVGI SIGIASSVHA EKSQTRLPVD DVRMLSQVLD
RIKQAYVEDI DDSELIESAI EGMLSGLDPH SDYLTPEDFA DLRESTSGEY GGLGIEITLD
ETGFIRVVAP IDDTPAFRAG MQSGDLITQI DDTPVKGMTV NDAVTLMRGE PGDPIELTVV
RDGENQPLVI EIVRDVIQIT SVRHRMLDDN FGYVRISQFQ ERTGRDFVDA MSELRSENGA
PLDGMVLDLR NNPGGVLQAS VEVVDALISE GLIVYTEGRL PNSASRFRAH SQDPSEGVNL
VVLINGGSAS ASEIVAGAVQ DHHRGIIMGT RSFGKGSVQT ILPLDENHAI KLTTARYFTP
SGRSIQAQGI VPDIEVRPGK LTQENGNPYY TEADLAGHLA NPEGENGSDD RADDSSETDE
QLIADYQLYQ ALTVLKGMRF LNGSR
//
