ID A0A014MAL4_9GAMM Unreviewed; 191 AA.
AC A0A014MAL4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:EXU75129.1};
GN Name=spr {ECO:0000313|EMBL:EXU75129.1};
GN ORFNames=BG55_12720 {ECO:0000313|EMBL:EXU75129.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75129.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75129.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75129.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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}.
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:EXU75129.1}.
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DR EMBL; JFHN01000051; EXU75129.1; -; Genomic_DNA.
DR RefSeq; WP_034937955.1; NZ_JFHN01000051.1.
DR AlphaFoldDB; A0A014MAL4; -.
DR STRING; 69222.BG55_12720; -.
DR PATRIC; fig|69222.5.peg.2619; -.
DR OrthoDB; 9807055at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019918};
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_5001472282"
FT DOMAIN 65..186
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 191 AA; 21493 MW; EC3EC9D7F52DE636 CRC64;
MVKSQPILRY IWRVIPAVAL ATLLSACSST NTGNNAQTDT HAVKDKNGFL LQASQDEFEQ
LVQNVDIKSR LMEQYSDWKG VRYRLGGTSK RGIDCSAFVQ TTFREQFGLD LPRSTYEQED
SGKSIQRAKL RPGDLVLLRA GSTGRHVGIY LGNDNFVHAS TSNGVMISNL NEAYWKNRYR
DARRVLSRSQ S
//
