ID C6DED8_PECCP Unreviewed; 622 AA.
AC C6DED8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Peptidase M3A and M3B thimet/oligopeptidase F {ECO:0000313|EMBL:ACT12623.1};
GN OrderedLocusNames=PC1_1581 {ECO:0000313|EMBL:ACT12623.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT12623.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT12623.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT12623.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP001657; ACT12623.1; -; Genomic_DNA.
DR RefSeq; WP_015839845.1; NC_012917.1.
DR AlphaFoldDB; C6DED8; -.
DR STRING; 561230.PC1_1581; -.
DR KEGG; pct:PC1_1581; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_031103_0_0_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1370.30; -; 2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 152..553
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 622 AA; 70695 MW; 45ABD100AD5FECF3 CRC64;
MQQVADYFNA LNRDYLAVHQ AKEELFWQLY MGTGDDEVSE RFSAAESAYK RFISQPRRLA
ELRTQLATLE SSPRDEQQQA LLHGLQGWYR FFDCNVIEDP QAQALMDEII AAESALYAKR
KSYEMTHLDA KGERVSASLG ELLTNQTTND TEAYRQSSQQ ALRDLEQWLL QNGFPELISL
RNRFARQMGY RNYFDYKVNK TERMTPEQLF AILDPFEEQT REANARSLKN LANEKGEDAL
QPWNIRYASA GDVTRQLDPY FPFSASLERW INSFKRLRIG FNGAEMQLDL LVRKGKYENG
FMHGPVPPFV QEGKWLPAQI NFTSLAKPDQ IGSGASGINT LFHEGGHAAH FANIKQNAPC
FSQEFPPTSM AYAETQSMFC DSLLGDADWL KRYAKNTQGE TIPDELIRAD ISTQQPMRAF
NERHILLVPY FEWQLYSWDD EARTPEAMTK LARDTEQRIL GISGSPRPTL AIPHLLSMES
ACSYQGYLLA LMAVEQTRSY FLQRDGYLTD NPAIGPDLAQ HYWLPGNSVS HDDTLRSLTG
EGFNPAYLAQ ACNLTVDEAW QQAQGTMTQA AARPQPAADF DLSAHIRVVD GSRVLADNAQ
GDEKMCQDFA AFIEREYPRS QA
//
