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Protein

Metalloprotease PmbA

Gene

pmbA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).1 Publication

Miscellaneous

In strains containing the pMccB17 plasmid, required for the maturation and secretion of the antibiotic bacteriocin microcin B17 (MccB17).1 Publication

GO - Molecular functioni

GO - Biological processi

  • proteolysis Source: EcoCyc

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease

Enzyme and pathway databases

BioCyciEcoCyc:EG10741-MONOMER.

Protein family/group databases

MEROPSiU62.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloprotease PmbA (EC:3.4.-.-)
Alternative name(s):
Protein TldE
Gene namesi
Name:pmbA
Synonyms:tldE
Ordered Locus Names:b4235, JW4194
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10741. pmbA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001423511 – 450Metalloprotease PmbAAdd BLAST450

Proteomic databases

EPDiP0AFK0.
PaxDbiP0AFK0.
PRIDEiP0AFK0.

Interactioni

Protein-protein interaction databases

BioGridi4262248. 15 interactors.
DIPiDIP-47844N.
IntActiP0AFK0. 6 interactors.
STRINGi316385.ECDH10B_4430.

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 30Combined sources22
Beta strandi34 – 51Combined sources18
Beta strandi54 – 72Combined sources19
Beta strandi75 – 82Combined sources8
Helixi86 – 100Combined sources15
Helixi114 – 116Combined sources3
Helixi134 – 149Combined sources16
Beta strandi155 – 174Combined sources20
Beta strandi179 – 197Combined sources19
Beta strandi200 – 212Combined sources13
Helixi213 – 215Combined sources3
Helixi219 – 232Combined sources14
Beta strandi241 – 248Combined sources8
Helixi250 – 264Combined sources15
Helixi266 – 270Combined sources5
Turni275 – 278Combined sources4
Beta strandi291 – 293Combined sources3
Beta strandi316 – 320Combined sources5
Helixi331 – 336Combined sources6
Helixi360 – 367Combined sources8
Beta strandi369 – 378Combined sources10
Turni383 – 385Combined sources3
Beta strandi387 – 398Combined sources12
Beta strandi401 – 414Combined sources14
Helixi415 – 420Combined sources6
Beta strandi432 – 436Combined sources5
Beta strandi440 – 448Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5NJ5X-ray1.90B/D1-450[»]
5NJ9X-ray1.25B/D1-450[»]
5NJAX-ray1.40B/D1-450[»]
5NJBX-ray1.50B/D1-450[»]
5NJCX-ray1.35B/D1-450[»]
5NJFX-ray1.42B/D1-450[»]
ProteinModelPortaliP0AFK0.
SMRiP0AFK0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase U62 family.Curated

Phylogenomic databases

eggNOGiENOG4105CMS. Bacteria.
COG0312. LUCA.
HOGENOMiHOG000224928.
InParanoidiP0AFK0.
KOiK03592.
OMAiMERDYDY.
PhylomeDBiP0AFK0.

Family and domain databases

Gene3Di3.30.2290.10. 1 hit.
InterProiView protein in InterPro
IPR002510. TldD/PmbA.
IPR035068. TldD/PmbA_N.
IPR036059. TldD/PmbA_sf.
PfamiView protein in Pfam
PF01523. PmbA_TldD. 1 hit.
SUPFAMiSSF111283. SSF111283. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALAMKVISQ VEAQRKILEE AVSTALELAS GKSDGAEVAV SKTTGISVST
60 70 80 90 100
RYGEVENVEF NSDGALGITV YHQNRKGSAS STDLSPQAIA RTVQAALDIA
110 120 130 140 150
RYTSPDPCAG VADKELLAFD APDLDLFHPA EVSPDEAIEL AARAEQAALQ
160 170 180 190 200
ADKRITNTEG GSFNSHYGVK VFGNSHGMLQ GYCSTRHSLS SCVIAEENGD
210 220 230 240 250
MERDYAYTIG RAMSDLQTPE WVGADCARRT LSRLSPRKLS TMKAPVIFAN
260 270 280 290 300
EVATGLFGHL VGAIAGGSVY RKSTFLLDSL GKQILPDWLT IEEHPHLLKG
310 320 330 340 350
LASTPFDSEG VRTERRDIIK DGILTQWLLT SYSARKLGLK STGHAGGIHN
360 370 380 390 400
WRIAGQGLSF EQMLKEMGTG LVVTELMGQG VSAITGDYSR GAAGFWVENG
410 420 430 440 450
EIQYPVSEIT IAGNLKDMWR NIVTVGNDIE TRSNIQCGSV LLPEMKIAGQ
Length:450
Mass (Da):48,370
Last modified:December 20, 2005 - v1
Checksum:iA062969197B52B5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54152 Genomic DNA. Translation: CAA38091.1.
D44452 Genomic DNA. Translation: BAA07915.1.
U14003 Genomic DNA. Translation: AAA97132.1.
U00096 Genomic DNA. Translation: AAC77192.1.
AP009048 Genomic DNA. Translation: BAE78235.1.
PIRiS13730.
RefSeqiNP_418656.1. NC_000913.3.
WP_001162171.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77192; AAC77192; b4235.
BAE78235; BAE78235; BAE78235.
GeneIDi948750.
KEGGiecj:JW4194.
eco:b4235.
PATRICifig|1411691.4.peg.2467.

Similar proteinsi

Entry informationi

Entry nameiPMBA_ECOLI
AccessioniPrimary (citable) accession number: P0AFK0
Secondary accession number(s): P24231, Q2M671
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome