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Protein

Penicillin-binding protein 1A

Gene

ponA1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (By similarity). Has little peptidoglycan hydrolytic activity; however it inhibits the synergistic peptidoglycan hydrolysis of RipA plus RpfB.By similarity1 Publication

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 sitei487Acyl-ester intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-4164-MONOMER.
UniPathwayiUPA00219.

Protein family/group databases

CAZyiGT51. Glycosyltransferase Family 51.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 1A
Short name:
PBP-1A
Alternative name(s):
Penicillin-binding protein 1*
Gene namesi
Name:ponA1
Ordered Locus Names:Rv0050
ORF Names:MTCY21D4.13
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0050.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004211241 – 820Penicillin-binding protein 1AAdd BLAST820

Proteomic databases

PaxDbiP71707.
PRIDEiP71707.

Interactioni

Subunit structurei

Interacts with RipA via its transpeptidase domain (residues 561-820).1 Publication

Protein-protein interaction databases

STRINGi83332.Rv0050.

Structurei

Secondary structure

1820
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi392 – 409Combined sources18
Helixi413 – 419Combined sources7
Beta strandi422 – 425Combined sources4
Helixi429 – 443Combined sources15
Beta strandi450 – 457Combined sources8
Turni459 – 461Combined sources3
Beta strandi463 – 468Combined sources6
Helixi486 – 489Combined sources4
Helixi490 – 499Combined sources10
Beta strandi507 – 509Combined sources3
Beta strandi513 – 515Combined sources3
Beta strandi518 – 520Combined sources3
Helixi523 – 525Combined sources3
Beta strandi529 – 532Combined sources4
Helixi533 – 539Combined sources7
Helixi542 – 551Combined sources10
Helixi555 – 566Combined sources12
Beta strandi575 – 577Combined sources3
Beta strandi583 – 585Combined sources3
Helixi590 – 594Combined sources5
Beta strandi597 – 599Combined sources3
Helixi601 – 612Combined sources12
Turni613 – 615Combined sources3
Beta strandi621 – 627Combined sources7
Beta strandi633 – 636Combined sources4
Turni637 – 639Combined sources3
Helixi650 – 660Combined sources11
Helixi663 – 666Combined sources4
Helixi673 – 675Combined sources3
Beta strandi679 – 686Combined sources8
Beta strandi690 – 702Combined sources13
Beta strandi705 – 716Combined sources12
Turni730 – 732Combined sources3
Helixi733 – 746Combined sources14
Beta strandi763 – 766Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5CRFX-ray1.80A/B/C/D391-820[»]
5CXWX-ray1.75A391-820[»]
ProteinModelPortaliP71707.
SMRiP71707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 360TransglycosylaseAdd BLAST181
Regioni453 – 743TranspeptidaseAdd BLAST291

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi63 – 123Pro-richAdd BLAST61
Compositional biasi767 – 820Pro-richAdd BLAST54

Domaini

A penicillin-binding domain is found between residues 420-820.

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 51 family.Curated
In the C-terminal section; belongs to the transpeptidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZ4. Bacteria.
COG0744. LUCA.
HOGENOMiHOG000041137.
InParanoidiP71707.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF56601. SSF56601. 2 hits.

Sequencei

Sequence statusi: Complete.

P71707-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSDGRHHQS SSGAPRGPAN PGQRGQVPPD DRLTAILPPV TDDRSAPHAD
60 70 80 90 100
SIEAVKAALD GAPPMPPPRD PLEEVTAALA APPGKPPRGD QLGGRRRPPG
110 120 130 140 150
PPGPPGSSGQ PAGRLPQPRV DLPRVGQINW KWIRRSLYLT AAVVILLPMV
160 170 180 190 200
TFTMAYLIVD VPKPGDIRTN QVSTILASDG SEIAKIVPPE GNRVDVNLSQ
210 220 230 240 250
VPMHVRQAVI AAEDRNFYSN PGFSFTGFAR AVKNNLFGGD LQGGSTITQQ
260 270 280 290 300
YVKNALVGSA QHGWSGLMRK AKELVIATKM SGEWSKDDVL QAYLNIIYFG
310 320 330 340 350
RGAYGISAAS KAYFDKPVEQ LTVAEGALLA ALIRRPSTLD PAVDPEGAHA
360 370 380 390 400
RWNWVLDGMV ETKALSPNDR AAQVFPETVP PDLARAENQT KGPNGLIERQ
410 420 430 440 450
VTRELLELFN IDEQTLNTQG LVVTTTIDPQ AQRAAEKAVA KYLDGQDPDM
460 470 480 490 500
RAAVVSIDPH NGAVRAYYGG DNANGFDFAQ AGLQTGSSFK VFALVAALEQ
510 520 530 540 550
GIGLGYQVDS SPLTVDGIKI TNVEGEGCGT CNIAEALKMS LNTSYYRLML
560 570 580 590 600
KLNGGPQAVA DAAHQAGIAS SFPGVAHTLS EDGKGGPPNN GIVLGQYQTR
610 620 630 640 650
VIDMASAYAT LAASGIYHPP HFVQKVVSAN GQVLFDASTA DNTGDQRIPK
660 670 680 690 700
AVADNVTAAM EPIAGYSRGH NLAGGRDSAA KTGTTQFGDT TANKDAWMVG
710 720 730 740 750
YTPSLSTAVW VGTVKGDEPL VTASGAAIYG SGLPSDIWKA TMDGALKGTS
760 770 780 790 800
NETFPKPTEV GGYAGVPPPP PPPEVPPSET VIQPTVEIAP GITIPIGPPT
810 820
TITLAPPPPA PPAATPTPPP
Length:820
Mass (Da):85,969
Last modified:February 6, 2013 - v3
Checksum:i6DD7A149081D3EB4
GO

Sequence cautioni

The sequence CCP42772 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42772.1. Different initiation.
PIRiB70913.
RefSeqiYP_177687.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP42772; CCP42772; Rv0050.
GeneIDi887065.
KEGGimtu:Rv0050.
PATRICi18148605. VBIMycTub87468_0056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP42772.1. Different initiation.
PIRiB70913.
RefSeqiYP_177687.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5CRFX-ray1.80A/B/C/D391-820[»]
5CXWX-ray1.75A391-820[»]
ProteinModelPortaliP71707.
SMRiP71707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0050.

Protein family/group databases

CAZyiGT51. Glycosyltransferase Family 51.

Proteomic databases

PaxDbiP71707.
PRIDEiP71707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP42772; CCP42772; Rv0050.
GeneIDi887065.
KEGGimtu:Rv0050.
PATRICi18148605. VBIMycTub87468_0056.

Organism-specific databases

TubercuListiRv0050.

Phylogenomic databases

eggNOGiENOG4105BZ4. Bacteria.
COG0744. LUCA.
HOGENOMiHOG000041137.
InParanoidiP71707.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciMTBH37RV:G185E-4164-MONOMER.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF56601. SSF56601. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiPBP1A_MYCTU
AccessioniPrimary (citable) accession number: P71707
Secondary accession number(s): L0T5D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: February 6, 2013
Last modified: November 2, 2016
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.