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Protein

Penicillin-binding protein 2

Gene

penA

Organism
Neisseria gonorrhoeae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesis of cross-linked peptidoglycan from the lipid intermediates.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei310Acyl-ester intermediate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 2
Short name:
PBP-2
Gene namesi
Name:penA
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei28 – 48HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB00535. Cefdinir.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001954491 – 581Penicillin-binding protein 2Add BLAST581

Interactioni

Protein-protein interaction databases

STRINGi528357.NgonPI_010100006000.

Structurei

Secondary structure

1581
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi55 – 57Combined sources3
Beta strandi65 – 71Combined sources7
Beta strandi85 – 91Combined sources7
Beta strandi165 – 168Combined sources4
Helixi172 – 175Combined sources4
Helixi176 – 179Combined sources4
Beta strandi188 – 190Combined sources3
Helixi191 – 195Combined sources5
Helixi197 – 201Combined sources5
Beta strandi205 – 211Combined sources7
Beta strandi217 – 220Combined sources4
Beta strandi235 – 238Combined sources4
Helixi241 – 257Combined sources17
Beta strandi261 – 269Combined sources9
Turni270 – 272Combined sources3
Beta strandi274 – 282Combined sources9
Helixi289 – 291Combined sources3
Helixi294 – 297Combined sources4
Helixi300 – 303Combined sources4
Helixi309 – 312Combined sources4
Helixi313 – 322Combined sources10
Beta strandi331 – 333Combined sources3
Beta strandi337 – 339Combined sources3
Beta strandi342 – 344Combined sources3
Beta strandi351 – 354Combined sources4
Helixi355 – 360Combined sources6
Helixi364 – 371Combined sources8
Helixi376 – 385Combined sources10
Turni386 – 389Combined sources4
Helixi407 – 409Combined sources3
Helixi412 – 419Combined sources8
Helixi428 – 439Combined sources12
Turni440 – 442Combined sources3
Beta strandi448 – 450Combined sources3
Helixi464 – 475Combined sources12
Turni476 – 478Combined sources3
Helixi485 – 487Combined sources3
Beta strandi495 – 505Combined sources11
Beta strandi507 – 509Combined sources3
Beta strandi511 – 526Combined sources16
Beta strandi529 – 537Combined sources9
Helixi547 – 563Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EQUX-ray2.40A/B44-581[»]
3EQVX-ray2.40A/B44-581[»]
4U3TX-ray2.20A/B237-574[»]
ProteinModelPortaliP08149.
SMRiP08149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08149.

Family & Domainsi

Domaini

The enzyme has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a C-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).

Sequence similaritiesi

Belongs to the transpeptidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CJN. Bacteria.
COG0768. LUCA.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

P08149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIKSEYKPR MLPKEEQVKK PMTSNGRISF VLMAMAVLFA CLIARGLYLQ
60 70 80 90 100
TVTYNFLKEQ GDNRIVRTQA LPATRGTVSD RNGAVLALSA PTESLFAVPK
110 120 130 140 150
DMKEMPSAAQ LERLSELVDV PVDVLRNKLE QKGKSFIWIK RQLDPKVAEE
160 170 180 190 200
VKALGLENFV FEKELKRHYP MGNLFAHVIG FTDIDGKGQE GLELSLEDSL
210 220 230 240 250
YGEDGAEVVL RDRQGNIVDS LDSPRNKAPQ NGKDIILSLD QRIQTLAYEE
260 270 280 290 300
LNKAVEYHQA KAGTVVVLDA RTGEILALAN TPAYDPNRPG RADSEQRRNR
310 320 330 340 350
AVTDMIEPGS AIKPFVIAKA LDAGKTDLNE RLNTQPYKIG PSPVRDTHVY
360 370 380 390 400
PSLDVRGIMQ KSSNVGTSKL SARFGAEEMY DFYHELGIGV RMHSGFPGET
410 420 430 440 450
AGLLRNWRRW RPIEQATMSF GYGLQLSLLQ LARAYTALTH DGVLLPLSFE
460 470 480 490 500
KQAVAPQGKR IFKESTAREV RNLMVSVTEP GGTGTAGAVD GFDVGAKTGT
510 520 530 540 550
ARKFVNGRYA DNKHVATFIG FAPAKNPRVI VAVTIDEPTA HGYYGGVVAG
560 570 580
PPFKKIMGGS LNILGISPTK PLTAAAVKTP S
Length:581
Mass (Da):63,650
Last modified:August 1, 1988 - v1
Checksum:iA495A788E465EFA2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti346D → DD in strain: CDC84-060418, CDC77-124615 and CDC84-060384. 1
Natural varianti504F → L in strain: CDC84-060418, CDC77-124615 and CDC84-060384. 1
Natural varianti510A → V in strain: CDC84-060418, CDC77-124615 and CDC84-060384. 1
Natural varianti516A → G in strain: CDC84-060418, CDC77-124615 and CDC84-060384. 1
Natural varianti541H → N in strain: FA19 and CDC84-060418. 1
Natural varianti551P → L in strain: CDC84-060384. 1
Natural varianti551P → S in strain: CDC77-124615. 1
Natural varianti552P → V in strain: CDC84-060418. 1
Natural varianti555 – 556KI → QV in strain: CDC84-060418. 2
Natural varianti566I → V in strain: CDC84-060418. 1
Natural varianti574A → NV in strain: CDC84-060418. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32091 Genomic DNA. Translation: AAA25463.1.
X07468 Genomic DNA. Translation: CAA30356.1.
X07469 Genomic DNA. Translation: CAA30357.1.
X07470 Genomic DNA. Translation: CAA30358.1.
PIRiS00916.
RefSeqiWP_003695531.1. NZ_CQOV01000014.1.
WP_003703066.1. NZ_JIBZ01000013.1.
WP_010360711.1. NZ_CQOD01000014.1.
WP_047917829.1. NZ_CQMS01000012.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32091 Genomic DNA. Translation: AAA25463.1.
X07468 Genomic DNA. Translation: CAA30356.1.
X07469 Genomic DNA. Translation: CAA30357.1.
X07470 Genomic DNA. Translation: CAA30358.1.
PIRiS00916.
RefSeqiWP_003695531.1. NZ_CQOV01000014.1.
WP_003703066.1. NZ_JIBZ01000013.1.
WP_010360711.1. NZ_CQOD01000014.1.
WP_047917829.1. NZ_CQMS01000012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EQUX-ray2.40A/B44-581[»]
3EQVX-ray2.40A/B44-581[»]
4U3TX-ray2.20A/B237-574[»]
ProteinModelPortaliP08149.
SMRiP08149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi528357.NgonPI_010100006000.

Chemistry databases

DrugBankiDB00535. Cefdinir.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CJN. Bacteria.
COG0768. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00219.

Miscellaneous databases

EvolutionaryTraceiP08149.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPBP2_NEIGO
AccessioniPrimary (citable) accession number: P08149
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein was sequenced in penicillin-sensitive strains LM306, and FA19, and in penicillin-resistant strains CDC84-060384, CDC84-060418 and CDC77-124615. The sequence shown is that of strain LM306.

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.