Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05364

- AMPC_ENTCL

UniProt

P05364 - AMPC_ENTCL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-lactamase

Gene

ampC

Organism
Enterobacter cloacae
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841Acyl-ester intermediate
Active sitei170 – 1701Proton acceptor

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

SABIO-RKP05364.

Protein family/group databases

MEROPSiS12.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase (EC:3.5.2.6)
Alternative name(s):
Cephalosporinase
Gene namesi
Name:ampC
OrganismiEnterobacter cloacae
Taxonomic identifieri550 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 381361Beta-lactamasePRO_0000016959Add
BLAST

Interactioni

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 4218
Beta strandi46 – 549
Beta strandi57 – 6711
Turni68 – 714
Beta strandi79 – 813
Helixi83 – 853
Helixi86 – 9914
Helixi109 – 1124
Helixi119 – 1213
Helixi126 – 1305
Helixi148 – 15710
Beta strandi166 – 1683
Helixi172 – 18211
Helixi184 – 1863
Helixi190 – 1978
Turni198 – 2036
Beta strandi207 – 2104
Helixi213 – 2186
Beta strandi222 – 2243
Beta strandi227 – 2293
Helixi237 – 2415
Helixi247 – 25812
Helixi260 – 2623
Helixi266 – 27510
Beta strandi277 – 2826
Beta strandi285 – 2873
Beta strandi292 – 2976
Helixi300 – 3078
Helixi309 – 3124
Beta strandi319 – 3257
Beta strandi329 – 33810
Beta strandi343 – 3497
Helixi350 – 3523
Beta strandi354 – 3629
Helixi366 – 37914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLSX-ray2.30A/B21-381[»]
1GCEX-ray1.80A21-381[»]
1RGZX-ray1.37A22-381[»]
1XX2X-ray1.88A/B21-381[»]
1Y54X-ray2.10A21-381[»]
2Q9MX-ray2.05A22-380[»]
2Q9NX-ray2.20A22-380[»]
3S4XX-ray1.95A21-381[»]
ProteinModelPortaliP05364.
SMRiP05364. Positions 22-380.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05364.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni335 – 3373Substrate binding

Sequence similaritiesi

Belongs to the class-C beta-lactamase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05364-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMRKSLCCAL LLGISCSALA TPVSEKQLAE VVANTITPLM KAQSVPGMAV
60 70 80 90 100
AVIYQGKPHY YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR
110 120 130 140 150
GEISLDDAVT RYWPQLTGKQ WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS
160 170 180 190 200
LLRFYQNWQP QWKPGTTRLY ANASIGLFGA LAVKPSGMPY EQAMTTRVLK
210 220 230 240 250
PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGMLDAQA YGVKTNVQDM
260 270 280 290 300
ANWVMANMAP ENVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA
310 320 330 340 350
NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP
360 370 380
EKQIGIVMLA NTSYPNPARV EAAYHILEAL Q
Length:381
Mass (Da):41,302
Last modified:November 1, 1988 - v1
Checksum:i90F56ABAF07AA304
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → I in strain: MHN1.
Natural varianti14 – 141I → L in strain: MHN1.
Natural varianti21 – 211T → A in strain: MHN1.
Natural varianti36 – 361I → V in strain: MHN1 and Q980R.
Natural varianti58 – 581P → S in strain: MHN1.
Natural varianti108 – 1081A → P in strain: MHN1 and Q980R.
Natural varianti152 – 1521L → V in strain: Q980R.
Natural varianti262 – 2621N → K in strain: MHN1.
Natural varianti319 – 3191A → V in strain: Q980R.
Natural varianti362 – 3621T → K in strain: MHN1.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07274 Genomic DNA. Translation: CAA30257.1.
X08082 Genomic DNA. Translation: CAA30879.1.
X08081 Genomic DNA. Translation: CAA30878.1.
PIRiS00404. PNKBP.
S00405. PNKBQ.
S00406. PNKBM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07274 Genomic DNA. Translation: CAA30257.1 .
X08082 Genomic DNA. Translation: CAA30879.1 .
X08081 Genomic DNA. Translation: CAA30878.1 .
PIRi S00404. PNKBP.
S00405. PNKBQ.
S00406. PNKBM.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BLS X-ray 2.30 A/B 21-381 [» ]
1GCE X-ray 1.80 A 21-381 [» ]
1RGZ X-ray 1.37 A 22-381 [» ]
1XX2 X-ray 1.88 A/B 21-381 [» ]
1Y54 X-ray 2.10 A 21-381 [» ]
2Q9M X-ray 2.05 A 22-380 [» ]
2Q9N X-ray 2.20 A 22-380 [» ]
3S4X X-ray 1.95 A 21-381 [» ]
ProteinModelPortali P05364.
SMRi P05364. Positions 22-380.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P05364.
ChEMBLi CHEMBL2725.

Protein family/group databases

MEROPSi S12.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P05364.

Miscellaneous databases

EvolutionaryTracei P05364.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view ]
Pfami PF00144. Beta-lactamase. 1 hit.
[Graphical view ]
SUPFAMi SSF56601. SSF56601. 1 hit.
PROSITEi PS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence and comparative analysis of three Enterobacter cloacae ampC beta-lactamase genes and their products."
    Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., Frere J.-M.
    Biochem. J. 250:753-760(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MHN1, P99 and Q908R.
  2. "Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase."
    Lobkovsky E., Moews P.C., Liu H., Zhao H., Frere J.-M., Knox J.R.
    Proc. Natl. Acad. Sci. U.S.A. 90:11257-11261(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Strain: P99.
  3. "Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog."
    Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., Knox J.R.
    Biochemistry 33:6762-6772(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Strain: P99.

Entry informationi

Entry nameiAMPC_ENTCL
AccessioniPrimary (citable) accession number: P05364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 1, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of strain P99.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3