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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)DescriptionActionsGraphical viewLength
Active sitei337Acyl-ester intermediateBy similarity1

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

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)DescriptionActionsGraphical viewLength
Transmembranei29 – 49HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi289M → T in C506; cefotamine resistant. 1 Publication1
Mutagenesisi597G → D in C506; cefotamine resistant. 1 Publication1
Mutagenesisi601G → V in C506; cefotamine resistant. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1255138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001954541 – 750Penicillin-binding protein 2XAdd BLAST750

Proteomic databases

PRIDEiP59676.

Interactioni

Protein-protein interaction databases

STRINGi171101.spr0304.

Chemistry databases

BindingDBiP59676.

Structurei

Secondary structure

1750
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi86 – 90Combined sources5
Helixi122 – 129Combined sources8
Helixi134 – 139Combined sources6
Beta strandi156 – 159Combined sources4
Turni160 – 162Combined sources3
Beta strandi191 – 194Combined sources4
Helixi195 – 198Combined sources4
Beta strandi201 – 205Combined sources5
Beta strandi211 – 215Combined sources5
Helixi218 – 222Combined sources5
Helixi224 – 228Combined sources5
Beta strandi260 – 264Combined sources5
Helixi267 – 284Combined sources18
Beta strandi287 – 295Combined sources9
Turni296 – 298Combined sources3
Beta strandi300 – 308Combined sources9
Turni312 – 314Combined sources3
Helixi327 – 330Combined sources4
Helixi336 – 339Combined sources4
Helixi340 – 349Combined sources10
Beta strandi358 – 360Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi369 – 371Combined sources3
Turni376 – 378Combined sources3
Beta strandi385 – 387Combined sources3
Helixi388 – 393Combined sources6
Helixi397 – 407Combined sources11
Helixi409 – 418Combined sources10
Turni419 – 422Combined sources4
Helixi442 – 447Combined sources6
Helixi448 – 450Combined sources3
Helixi458 – 469Combined sources12
Turni470 – 472Combined sources3
Beta strandi480 – 485Combined sources6
Helixi486 – 488Combined sources3
Beta strandi490 – 493Combined sources4
Beta strandi498 – 500Combined sources3
Helixi505 – 520Combined sources16
Turni522 – 524Combined sources3
Turni530 – 533Combined sources4
Beta strandi534 – 537Combined sources4
Beta strandi545 – 552Combined sources8
Beta strandi556 – 561Combined sources6
Beta strandi568 – 580Combined sources13
Beta strandi582 – 591Combined sources10
Helixi597 – 613Combined sources17
Helixi616 – 618Combined sources3
Turni626 – 629Combined sources4
Helixi646 – 655Combined sources10
Beta strandi659 – 665Combined sources7
Beta strandi667 – 674Combined sources8
Beta strandi685 – 691Combined sources7
Helixi704 – 713Combined sources10
Beta strandi717 – 722Combined sources6
Beta strandi725 – 732Combined sources8
Helixi738 – 740Combined sources3
Beta strandi742 – 749Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP59676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini632 – 691PASTA 1PROSITE-ProRule annotationAdd BLAST60
Domaini692 – 750PASTA 2PROSITE-ProRule annotationAdd BLAST59

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.
OMAiGTVHNQD.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PYYX-ray2.42A49-750[»]
ProteinModelPortaliP59676.
SMRiP59676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi171101.spr0304.

Chemistry databases

BindingDBiP59676.
ChEMBLiCHEMBL1255138.

Proteomic databases

PRIDEiP59676.

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.
OMAiGTVHNQD.

Miscellaneous databases

EvolutionaryTraceiP59676.
PROiP59676.

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...

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: November 2, 2016
This is version 106 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.