ID A0A2Z6E8N2_9GAMM Unreviewed; 445 AA.
AC A0A2Z6E8N2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:BBD80859.1};
GN ORFNames=ALSL_2233 {ECO:0000313|EMBL:BBD80859.1};
OS Aerosticca soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Aerosticca.
OX NCBI_TaxID=2010829 {ECO:0000313|EMBL:BBD80859.1, ECO:0000313|Proteomes:UP000270530};
RN [1] {ECO:0000313|Proteomes:UP000270530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dysh456 {ECO:0000313|Proteomes:UP000270530};
RA Watanabe M., Kojima H.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000270530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dysh456 {ECO:0000313|Proteomes:UP000270530};
RA Fukui M.;
RT "Genome sequence of Rhodanobacteraceae bacterium strain Dysh456.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; AP018560; BBD80859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6E8N2; -.
DR KEGG; rbd:ALSL_2233; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000270530; Chromosome.
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, ECO:0000313|EMBL:BBD80859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270530};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..445
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016361992"
FT DOMAIN 95..163
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 445 AA; 47052 MW; 48148CB447518E41 CRC64;
MRLLTCGLCL LLTAAPVLHG QDLPATAGSA PATAASTAAA DRISLDDIRN FSRVYEVIRQ
AYVEPVDNKT LMNAAISGML SGLDPHSAYL DKEGLEQLNE DTTGQYSGLG IEVMEVDGTL
RVIAPIDDTP ASRAGIKPGD TIIKIDGRPV DADNLDDMFK RLRGEPGTKV TLTIVHENGN
KPVDYSLVRE KISLASVKLR ALEPGYVYIR LSQFQEDTAD DLERKLADYV KKNGPPKGAI
LDLRSNPGGL LTAAVAVSDA FLDAGTIVTT RGRLQDANMQ FSAHPGDLLK GAPIVVLVDN
GTASAAEIVA GALKDNRRAL IMGRRTFGKG VVQTVLPLDA DHAVKLTTAR YYTPSGTSIQ
AEGIKPDIAL ADLAVNKADS PATLITSEAD LEHHLANEKA GTGKDIDNDG SAENAKLATE
DYALSQALNV LKAITLARTG ASSAH
//
