Penicillin-binding protein 2 - Staphylococcus aureus (strain bovine RF122 / ET3-1)

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Q2YY56 (Q2YY56_STAAB) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·Ontologies·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Penicillin-binding protein 2 EMBL CAI81003.1
EC=2.3.2.- EMBL CAI81003.1

Gene names

Name:	pbp2 EMBL CAI81003.1
Ordered Locus Names:	SAB1314

Organism

Staphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP] EMBL CAI81003.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Acyltransferase EMBL CAI81003.1 Transferase
Technical term	3D-structure PDB 2OLV PDB 2OLU Complete proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	peptidoglycan-based cell wall Inferred from electronic annotation. Source: InterPro
Molecular_function	penicillin binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring acyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q2YY56 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: E333F51105B2108F
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727

80,398

        10         20         30         40         50         60 
MTENKGSSQP KKNGNNGGKS NSKKNRNVKR TIIKIIGFMI IAFFVVLLLG ILLFAYYAWK 

        70         80         90        100        110        120 
APAFTEAKLQ DPIPAKIYDK NGELVKTLDN GQRHEHVNLK DVPKSMKDAV LATEDNRFYE 

       130        140        150        160        170        180 
HGALDYKRLF GAIGKNLTGG FGSEGASTLT QQVVKDAFLS QHKSIGRKAQ EAYLSYRLEQ 

       190        200        210        220        230        240 
EYSKDDIFQV YLNKIYYSDG VTGIKAAAKY YFNKDLKDLN LAEEAYLAGL PQVPNNYNIY 

       250        260        270        280        290        300 
DHPKAAEDRK NTVLYLMHYH KRITDKQWED AKKIDLKANL VNRTAEERQN IDTNQDSEYN 

       310        320        330        340        350        360 
SYVNFVKSEL MNNKAFKDEN LGNVLQSGIK IYTNMDKDVQ KTLQNDVDNG SFYKNKDQQV 

       370        380        390        400        410        420 
GATILDSKTG GLVAISGGRD FKDVVNRNQA TDPHPTGSSL KPFLAYGPAI ENMKWATNHA 

       430        440        450        460        470        480 
IQDESSYQVD GSTFRNYDVK SHGTVSIYDA LRQSFNIPAL KAWQSVKQNA GNDAPKKFAA 

       490        500        510        520        530        540 
KLGLNYEGDI GPSEVLGGSA SEFSPTQLAS AFAAIANGGT YNNAHSIQKV VTRDGETIEY 

       550        560        570        580        590        600 
DHTSHKAMSD YTAYMLAEML KGTFKPYGSA YGHGVSGVNM GAKTGTGTYG AETYSQYNLP 

       610        620        630        640        650        660 
DNAAKDVWIN GFTPQYTMSV WMGFSKVKQY GENSFVGHSQ QEYPQFLYEN VMSKISSRDG 

       670        680        690        700        710        720 
EDFKRPSSVS GSIPSINVSG SQDNNTTNRS THGGSDTSAN SSGTAQSNNN TRSQQSRNSG 


GLTGIFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular correlates of host specialization in Staphylococcus aureus." Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V. PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: bovine RF122 / ET3-1.
[2]	"Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis." Lovering A.L., de Castro L.H., Lim D., Strynadka N.C. Science 315:1402-1405(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 60-727.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ938182 Genomic DNA. Translation: CAI81003.1.

RefSeq

YP_416790.1. NC_007622.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OLU	X-ray	2.90	A	60-727	[»]
2OLV	X-ray	2.80	A/B	60-727	[»]

ProteinModelPortal

SMR

Q2YY56. Positions 67-692.

ModBase

Protein-protein interaction databases

STRING

273036.SAB1314.

Protein family/group databases

CAZy

GT51. Glycosyltransferase Family 51.

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

EnsemblBacteria

CAI81003; CAI81003; SAB1314.

GeneID

KEGG

PATRIC

19523509. VBIStaAur92441_1403.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

KO

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

SAUR273036:GJVS-1336-MONOMER.

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR001460. PCN-bd_Tpept.
[Graphical view]

Pfam

PF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

ProtoNet

Other

EvolutionaryTrace

Entry information

Entry name

Q2YY56_STAAB

Accession

Primary (citable) accession number: Q2YY56

Entry history

Integrated into UniProtKB/TrEMBL:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·Ontologies·Sequences·References·Cross-refs·Entry info