PMBA_ECO57
ID PMBA_ECO57 Reviewed; 450 AA.
AC P0AFK1; P24231;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Metalloprotease PmbA;
DE EC=3.4.-.-;
GN Name=pmbA; OrderedLocusNames=Z5845, ECs5212;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the
CC inhibitory activity of the carbon storage regulator (CsrA) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR EMBL; AE005174; AAG59432.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38635.1; -; Genomic_DNA.
DR PIR; D86121; D86121.
DR PIR; D91280; D91280.
DR RefSeq; NP_313239.1; NC_002695.1.
DR RefSeq; WP_001162171.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFK1; -.
DR SMR; P0AFK1; -.
DR STRING; 155864.EDL933_5582; -.
DR EnsemblBacteria; AAG59432; AAG59432; Z5845.
DR EnsemblBacteria; BAB38635; BAB38635; ECs_5212.
DR GeneID; 60903082; -.
DR GeneID; 913868; -.
DR KEGG; ece:Z5845; -.
DR KEGG; ecs:ECs_5212; -.
DR PATRIC; fig|386585.9.peg.5448; -.
DR eggNOG; COG0312; Bacteria.
DR HOGENOM; CLU_026425_0_0_6; -.
DR OMA; LYRKSTF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2290.10; -; 1.
DR InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR InterPro; IPR035068; TldD/PmbA_N.
DR InterPro; IPR036059; TldD/PmbA_sf.
DR Pfam; PF01523; PmbA_TldD; 1.
DR Pfam; PF19289; PmbA_TldD_C; 1.
DR Pfam; PF19290; PmbA_TldD_M; 1.
DR SUPFAM; SSF111283; SSF111283; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..450
FT /note="Metalloprotease PmbA"
FT /id="PRO_0000142352"
SQ SEQUENCE 450 AA; 48370 MW; A062969197B52B5E CRC64;
MALAMKVISQ VEAQRKILEE AVSTALELAS GKSDGAEVAV SKTTGISVST RYGEVENVEF
NSDGALGITV YHQNRKGSAS STDLSPQAIA RTVQAALDIA RYTSPDPCAG VADKELLAFD
APDLDLFHPA EVSPDEAIEL AARAEQAALQ ADKRITNTEG GSFNSHYGVK VFGNSHGMLQ
GYCSTRHSLS SCVIAEENGD MERDYAYTIG RAMSDLQTPE WVGADCARRT LSRLSPRKLS
TMKAPVIFAN EVATGLFGHL VGAIAGGSVY RKSTFLLDSL GKQILPDWLT IEEHPHLLKG
LASTPFDSEG VRTERRDIIK DGILTQWLLT SYSARKLGLK STGHAGGIHN WRIAGQGLSF
EQMLKEMGTG LVVTELMGQG VSAITGDYSR GAAGFWVENG EIQYPVSEIT IAGNLKDMWR
NIVTVGNDIE TRSNIQCGSV LLPEMKIAGQ