ID A1SWR3_PSYIN Unreviewed; 664 AA.
AC A1SWR3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=C-terminal processing peptidase-1, Serine peptidase, MEROPS family S41A {ECO:0000313|EMBL:ABM03928.1};
GN OrderedLocusNames=Ping_2187 {ECO:0000313|EMBL:ABM03928.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM03928.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM03928.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM03928.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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; CP000510; ABM03928.1; -; Genomic_DNA.
DR RefSeq; WP_011770488.1; NC_008709.1.
DR AlphaFoldDB; A1SWR3; -.
DR STRING; 357804.Ping_2187; -.
DR MEROPS; S41.001; -.
DR KEGG; pin:Ping_2187; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_016199_1_0_6; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000000639; 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 InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR PANTHER; PTHR32060:SF32; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF11818; DUF3340; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF17804; TSP_NTD; 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:UP000000639};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..664
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002637553"
FT DOMAIN 238..308
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 664 AA; 75338 MW; 3D10503599C3F47D CRC64;
MNKYFRHLAV IASYLYIGIV CAVPADFDSA DIPQLEQQAQ HAKVTKRVSD LFSRSHYKYI
PLNDALSQQV FERYIEQLDY NKQIFMQSDI NDLKSYQFLL DDNLKTGQLQ PAYEIYQLSL
KRRYERFSYA LSLLDKEIMF DTTDEFQFDR SKAPWAKDTV ELNKIWQQKV KSDALVLKLS
GKTWDKIKEL LSKRYNYALK HLTQTESEDV FQTFMNAYAR TIEPHTSYLS PRNAERFKME
MNLSLEGIGA VLQLEDDYTV IRSLVPGGPA ERSNQIFKND KIIGVGQEDG KVVDVVGWRL
DDIVDLIKGP KGTDVKLQIL SGKAGDKSKI VIITREQIHL EDREAKSSVE VIDGQKIGVI
TIPSFYMNLS EDVDQELALL AKENIKGIII DLRNNGGGAL SEATLLTGLF IGTGPVVQVR
DGRNQVLVHQ DENKAVSYKG PLTVLINRNS ASASEIFAAA LQDYGRAIIL GEQSFGKGTV
QQHRRISRFY DKDADLVGSV QYTIAKFYRI DGGSTQNKGV IPDIQFPSGI DPNETGESLE
KNALPWDNIK SADYSPVNNL QSVVKSLTEK HNLRIKNKIE FSYLEKDIEE YLQEKDMTTI
SLKESDRIKL REEQEKESLV RVNERLKRAG LPEVKSVDDI PDDFEPIDSF LLEAAAITLD
YAHS
//