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Protein

Penicillin-binding protein 2X

Gene

pbpX

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei337 – 3371Acyl-ester intermediateBy similarity

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

BioCyciSPNE171101:GJC8-311-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 2X
Short name:
PBP-2X
Short name:
PBP2X
Gene namesi
Name:pbpX
Ordered Locus Names:spr0304
OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
Taxonomic identifieri171101 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000586 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi289 – 2891M → T in C506; cefotamine resistant. 1 Publication
Mutagenesisi597 – 5971G → D in C506; cefotamine resistant. 1 Publication
Mutagenesisi601 – 6011G → V in C506; cefotamine resistant. 1 Publication

Chemistry

ChEMBLiCHEMBL1255138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750Penicillin-binding protein 2XPRO_0000195454Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi171101.spr0304.

Chemistry

BindingDBiP59676.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi86 – 905Combined sources
Helixi122 – 1298Combined sources
Helixi134 – 1396Combined sources
Beta strandi156 – 1594Combined sources
Turni160 – 1623Combined sources
Beta strandi191 – 1944Combined sources
Helixi195 – 1984Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi211 – 2155Combined sources
Helixi218 – 2225Combined sources
Helixi224 – 2285Combined sources
Beta strandi260 – 2645Combined sources
Helixi267 – 28418Combined sources
Beta strandi287 – 2959Combined sources
Turni296 – 2983Combined sources
Beta strandi300 – 3089Combined sources
Turni312 – 3143Combined sources
Helixi327 – 3304Combined sources
Helixi336 – 3394Combined sources
Helixi340 – 34910Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi369 – 3713Combined sources
Turni376 – 3783Combined sources
Beta strandi385 – 3873Combined sources
Helixi388 – 3936Combined sources
Helixi397 – 40711Combined sources
Helixi409 – 41810Combined sources
Turni419 – 4224Combined sources
Helixi442 – 4476Combined sources
Helixi448 – 4503Combined sources
Helixi458 – 46912Combined sources
Turni470 – 4723Combined sources
Beta strandi480 – 4856Combined sources
Helixi486 – 4883Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi498 – 5003Combined sources
Helixi505 – 52016Combined sources
Turni522 – 5243Combined sources
Turni530 – 5334Combined sources
Beta strandi534 – 5374Combined sources
Beta strandi545 – 5528Combined sources
Beta strandi556 – 5616Combined sources
Beta strandi568 – 58013Combined sources
Beta strandi582 – 59110Combined sources
Helixi597 – 61317Combined sources
Helixi616 – 6183Combined sources
Turni626 – 6294Combined sources
Helixi646 – 65510Combined sources
Beta strandi659 – 6657Combined sources
Beta strandi667 – 6748Combined sources
Beta strandi685 – 6917Combined sources
Helixi704 – 71310Combined sources
Beta strandi717 – 7226Combined sources
Beta strandi725 – 7328Combined sources
Helixi738 – 7403Combined sources
Beta strandi742 – 7498Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PYYX-ray2.42A49-750[»]
ProteinModelPortaliP59676.
SMRiP59676. Positions 64-750.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini632 – 69160PASTA 1PROSITE-ProRule annotationAdd
BLAST
Domaini692 – 75059PASTA 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transpeptidase family.Curated
Contains 2 PASTA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CJN. Bacteria.
COG0768. LUCA.
HOGENOMiHOG000049551.
KOiK12556.
OMAiGRSQVEF.
OrthoDBiEOG6N0HHV.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005543. PASTA_dom.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03793. PASTA. 1 hit.
PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
PROSITEiPS51178. PASTA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWTKRVIRY ATKNRKSPAE NRRRVGKSLS LLSVFVFAIF LVNFAVIIGT
60 70 80 90 100
GTRFGTDLAK EAKKVHQTTR TVPAKRGTIY DRNGVPIAED ATSYNVYAVI
110 120 130 140 150
DENYKSATGK ILYVEKTQFN KVAEVFHKYL DMEESYVREQ LSQPNLKQVS
160 170 180 190 200
FGAKGNGITY ANMMSIKKEL EAAEVKGIDF TTSPNRSYPN GQFASSFIGL
210 220 230 240 250
AQLHENEDGS KSLLGTSGME SSLNSILAGT DGIITYEKDR LGNIVPGTEQ
260 270 280 290 300
VSQRTMDGKD VYTTISSPLQ SFMETQMDAF QEKVKGKYMT ATLVSAKTGE
310 320 330 340 350
ILATTQRPTF DADTKEGITE DFVWRDILYQ SNYEPGSTMK VMMLAAAIDN
360 370 380 390 400
NTFPGGEVFN SSELKIADAT IRDWDVNEGL TGGRMMTFSQ GFAHSSNVGM
410 420 430 440 450
TLLEQKMGDA TWLDYLNRFK FGVPTRFGLT DEYAGQLPAD NIVNIAQSSF
460 470 480 490 500
GQGISVTQTQ MIRAFTAIAN DGVMLEPKFI SAIYDPNDQT ARKSQKEIVG
510 520 530 540 550
NPVSKDAASL TRTNMVLVGT DPVYGTMYNH STGKPTVTVP GQNVALKSGT
560 570 580 590 600
AQIADEKNGG YLVGLTDYIF SAVSMSPAEN PDFILYVTVQ QPEHYSGIQL
610 620 630 640 650
GEFANPILER ASAMKDSLNL QTTAKALEQV SQQSPYPMPS VKDISPGDLA
660 670 680 690 700
EELRRNLVQP IVVGTGTKIK NSSAEEGKNL APNQQVLILS DKAEEVPDMY
710 720 730 740 750
GWTKETAETL AKWLNIELEF QGSGSTVQKQ DVRANTAIKD IKKITLTLGD
Length:750
Mass (Da):82,343
Last modified:May 16, 2003 - v1
Checksum:i0699AF8081B25869
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16367 Genomic DNA. Translation: CAA34412.1.
AE007317 Genomic DNA. Translation: AAK99108.1.
RefSeqiNP_357898.1. NC_003098.1.
WP_000872267.1. NC_003098.1.

Genome annotation databases

EnsemblBacteriaiAAK99108; AAK99108; spr0304.
GeneIDi934744.
KEGGispr:spr0304.
PATRICi19700441. VBIStrPne107296_0341.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16367 Genomic DNA. Translation: CAA34412.1.
AE007317 Genomic DNA. Translation: AAK99108.1.
RefSeqiNP_357898.1. NC_003098.1.
WP_000872267.1. NC_003098.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PYYX-ray2.42A49-750[»]
ProteinModelPortaliP59676.
SMRiP59676. Positions 64-750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi171101.spr0304.

Chemistry

BindingDBiP59676.
ChEMBLiCHEMBL1255138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK99108; AAK99108; spr0304.
GeneIDi934744.
KEGGispr:spr0304.
PATRICi19700441. VBIStrPne107296_0341.

Phylogenomic databases

eggNOGiENOG4105CJN. Bacteria.
COG0768. LUCA.
HOGENOMiHOG000049551.
KOiK12556.
OMAiGRSQVEF.
OrthoDBiEOG6N0HHV.

Enzyme and pathway databases

BioCyciSPNE171101:GJC8-311-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP59676.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005543. PASTA_dom.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03793. PASTA. 1 hit.
PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SMARTiSM00740. PASTA. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
PROSITEiPS51178. PASTA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506."
    Laible G., Hakenbeck R., Sicard M.A., Joris B., Ghuysen J.-M.
    Mol. Microbiol. 3:1337-1348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-289; GLY-597 AND GLY-601.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-255 / R6.

Entry informationi

Entry nameiPBPX_STRR6
AccessioniPrimary (citable) accession number: P59676
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: December 9, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The mature form of PBP2x contains an unprocessed signal sequence followed by a membrane-anchoring segment.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.