ID E1SJ94_PANVC Unreviewed; 191 AA.
AC E1SJ94;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Lipoprotein spr {ECO:0000313|EMBL:ADO10232.1};
GN Name=spr {ECO:0000313|EMBL:ADO10232.1};
GN OrderedLocusNames=Pvag_2050 {ECO:0000313|EMBL:ADO10232.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10232.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO10232.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO10232.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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; CP002206; ADO10232.1; -; Genomic_DNA.
DR RefSeq; WP_013358530.1; NC_014562.1.
DR AlphaFoldDB; E1SJ94; -.
DR MEROPS; C40.004; -.
DR GeneID; 58737395; -.
DR KEGG; pva:Pvag_2050; -.
DR eggNOG; COG0791; Bacteria.
DR HOGENOM; CLU_016043_9_1_6; -.
DR OrthoDB; 9807055at2; -.
DR Proteomes; UP000006631; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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; MUREIN DD-ENDOPEPTIDASE MEPS/MUREIN LD-CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR47360:SF3; 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:ARBA00023288, ECO:0000313|EMBL:ADO10232.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..191
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003151092"
FT DOMAIN 65..186
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 191 AA; 21669 MW; 216BCDB50C74B8C4 CRC64;
MVKSQPILRY ILRIVPALAL ATLLSACSST HSSQNANNEN HEVNNHNGFL LQASQDEFEE
MVRNVDVKSR IMEQYAVWKG VRYRLGGDTK RGIDCSAFVQ RTFRDQFGLE LPRSTSEQQD
TGKEITRSKL RPGDLVMFRA GSTGRHVGIY LGNDNFVHAS TSSGVMISSL NDDYWKKRYR
EGRRVLSRNP T
//
