PMBA_ECOLI
ID PMBA_ECOLI Reviewed; 450 AA.
AC P0AFK0; P24231; Q2M671;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Metalloprotease PmbA;
DE EC=3.4.-.-;
DE AltName: Full=Protein TldE;
GN Name=pmbA; Synonyms=tldE; OrderedLocusNames=b4235, JW4194;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2082149; DOI=10.1111/j.1365-2958.1990.tb02041.x;
RA Rodriguez-Sainz M.C., Hernandez-Chico C., Moreno F.;
RT "Molecular characterization of pmbA, an Escherichia coli chromosomal gene
RT required for the production of the antibiotic peptide MccB17.";
RL Mol. Microbiol. 4:1921-1932(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=8604133; DOI=10.1006/jmbi.1996.0103;
RA Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T.,
RA Sekimizu K., Miki T.;
RT "Evidence for involvement of Escherichia coli genes pmbA, csrA and a
RT previously unrecognized gene tldD, in the control of DNA gyrase by letD
RT (ccdB) of sex factor F.";
RL J. Mol. Biol. 256:483-502(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=12029038; DOI=10.1128/jb.184.12.3224-3231.2002;
RA Allali N., Afif H., Couturier M., Van Melderen L.;
RT "The highly conserved TldD and TldE proteins of Escherichia coli are
RT involved in microcin B17 processing and in CcdA degradation.";
RL J. Bacteriol. 184:3224-3231(2002).
CC -!- FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the
CC inhibitory activity of the carbon storage regulator (CsrA).
CC {ECO:0000269|PubMed:12029038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In strains containing the pMccB17 plasmid, required for
CC the maturation and secretion of the antibiotic bacteriocin microcin B17
CC (MccB17). {ECO:0000305|PubMed:12029038}.
CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR EMBL; X54152; CAA38091.1; -; Genomic_DNA.
DR EMBL; D44452; BAA07915.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97132.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77192.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78235.1; -; Genomic_DNA.
DR PIR; S13730; S13730.
DR RefSeq; NP_418656.1; NC_000913.3.
DR RefSeq; WP_001162171.1; NZ_LN832404.1.
DR PDB; 5NJ5; X-ray; 1.90 A; B/D=1-450.
DR PDB; 5NJ9; X-ray; 1.25 A; B/D=1-450.
DR PDB; 5NJA; X-ray; 1.40 A; B/D=1-450.
DR PDB; 5NJB; X-ray; 1.50 A; B/D=1-450.
DR PDB; 5NJC; X-ray; 1.35 A; B/D=1-450.
DR PDB; 5NJF; X-ray; 1.42 A; B/D=1-450.
DR PDBsum; 5NJ5; -.
DR PDBsum; 5NJ9; -.
DR PDBsum; 5NJA; -.
DR PDBsum; 5NJB; -.
DR PDBsum; 5NJC; -.
DR PDBsum; 5NJF; -.
DR AlphaFoldDB; P0AFK0; -.
DR SMR; P0AFK0; -.
DR BioGRID; 4262248; 15.
DR DIP; DIP-47844N; -.
DR IntAct; P0AFK0; 6.
DR STRING; 511145.b4235; -.
DR jPOST; P0AFK0; -.
DR PaxDb; P0AFK0; -.
DR PRIDE; P0AFK0; -.
DR EnsemblBacteria; AAC77192; AAC77192; b4235.
DR EnsemblBacteria; BAE78235; BAE78235; BAE78235.
DR GeneID; 60903082; -.
DR GeneID; 948750; -.
DR KEGG; ecj:JW4194; -.
DR KEGG; eco:b4235; -.
DR PATRIC; fig|1411691.4.peg.2467; -.
DR EchoBASE; EB0734; -.
DR eggNOG; COG0312; Bacteria.
DR HOGENOM; CLU_026425_0_0_6; -.
DR InParanoid; P0AFK0; -.
DR OMA; LYRKSTF; -.
DR PhylomeDB; P0AFK0; -.
DR BioCyc; EcoCyc:EG10741-MON; -.
DR BioCyc; MetaCyc:107410-MON; -.
DR PRO; PR:P0AFK0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1905368; C:peptidase complex; IDA:EcoCyc.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..450
FT /note="Metalloprotease PmbA"
FT /id="PRO_0000142351"
FT HELIX 9..30
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 34..51
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 54..72
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 155..174
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 179..197
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 200..212
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:5NJ9"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:5NJ9"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 387..398
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 401..414
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:5NJ9"
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
