ID C6DGQ9_PECCP Unreviewed; 505 AA.
AC C6DGQ9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ACT11146.1};
GN OrderedLocusNames=PC1_0084 {ECO:0000313|EMBL:ACT11146.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT11146.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT11146.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT11146.1,
RC ECO:0000313|Proteomes:UP000002736};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP001657; ACT11146.1; -; Genomic_DNA.
DR RefSeq; WP_012772827.1; NC_012917.1.
DR AlphaFoldDB; C6DGQ9; -.
DR STRING; 561230.PC1_0084; -.
DR KEGG; pct:PC1_0084; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_043932_0_0_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..505
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002964344"
FT DOMAIN 51..165
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..377
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 474..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 56207 MW; 2F8CF36B3CF0772C CRC64;
MQGTKKALFV GGLLLAVVSS SVQAEALQPD PAWQQGKLDN GFTWQLLTTP QRPGDRVELR
LVVNAGSLLE NAQQVGFAHF LPRLALAPGD KLSAAQRPST WMSDANGSRV LPPAIISYDF
TSYNLSLPNN RPELLKEALT WLAESAGQMT FDEKSLQAAL KVPDQVATFP VNPQDPSWRY
RLKGSPLLAH DPAQDVKPPL NGEQLQQFYK TWYTPDAMTL YIVGHVDNRS VIEQIGKVFS
PLEGKREAPA PLPTLSPLPT QAISLMNNNV QKDTLSLMWD APWHPIRESQ ALVRYWLGDM
TREAMFWHLQ QVLEKSPQKG NNLRFDCNVF YTRSQCAIHM DVPNSEGVEP GVTFMARELA
TLREKGLTQQ EFDALIARKT DELNKLFATY ARTSTDILMD QRLRSQQNGV VDIAPEQYQK
LRQSYLSALT LDMLNQELHQ QLVQDTTLML IQQPGEPEAN MKALQEAYDR IMTPATEPAA
SAATAAPEGA VPEGKKPQET APAAQ
//
