ID A1STI4_PSYIN Unreviewed; 167 AA.
AC A1STI4;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=NLP/P60 protein {ECO:0000313|EMBL:ABM02799.1};
GN OrderedLocusNames=Ping_0958 {ECO:0000313|EMBL:ABM02799.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02799.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM02799.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM02799.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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DR EMBL; CP000510; ABM02799.1; -; Genomic_DNA.
DR RefSeq; WP_011769362.1; NC_008709.1.
DR AlphaFoldDB; A1STI4; -.
DR STRING; 357804.Ping_0958; -.
DR MEROPS; C40.004; -.
DR KEGG; pin:Ping_0958; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_9_3_6; -.
DR OrthoDB; 9807055at2; -.
DR Proteomes; UP000000639; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR47360:SF1; ENDOPEPTIDASE NLPC-RELATED; 1.
DR PANTHER; PTHR47360; MUREIN DD-ENDOPEPTIDASE MEPS/MUREIN LD-CARBOXYPEPTIDASE; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..167
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002637862"
FT DOMAIN 43..166
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 167 AA; 18712 MW; CB2D837AFC24D073 CRC64;
MVNKLKVSCC SIILLIMLSA CSSSSPVAGQ SESFKKITDG TLMEEVASVL LRNEFDIWEG
TPYRFGGTNK QGIDCSALIQ KIYLSSFNLK LPRTTKRQSR QGYLINKSKL QVGDLVFFKT
SLTDNHVGIF IGNGLFLHAS SSQGVMISVL NNSYWRSKYW QSRRILN
//
