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Protein

Penicillin-binding protein 4B

Gene

pbpI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Penicillin-binding protein with an unknown catalytic activity. Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei304 – 3041Acyl-ester intermediateBy similarity

GO - Molecular functioni

  1. penicillin binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU27310-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 4B
Short name:
PBP-4B
Short name:
PBP4b
Alternative name(s):
Penicillin-binding protein I
Gene namesi
Name:pbpI
Synonyms:yrrR
Ordered Locus Names:BSU27310
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU27310. [Micado]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 584552ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Spores have normal morphology, heat-resistance, cortex structure, and germination and outgrowth properties.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584Penicillin-binding protein 4BPRO_0000360667Add
BLAST

Proteomic databases

PaxDbiO32032.

Expressioni

Developmental stagei

Sporulation specific. Expression starts 1 to 2 hours after the initiation of sporulation. Found only in mother cells.

Interactioni

Protein-protein interaction databases

IntActiO32032. 1 interaction.
STRINGi224308.BSU27310.

Family & Domainsi

Sequence similaritiesi

Belongs to the transpeptidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0768.
HOGENOMiHOG000097173.
InParanoidiO32032.
OMAiKWFAGYF.
OrthoDBiEOG6N0HHV.
PhylomeDBiO32032.

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. 2 hits.

Sequencei

Sequence statusi: Complete.

O32032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKISKRMKLA VIAFLIVFFL LLLRLAEIQL FFTESFSKKK INLIQESVKQ
60 70 80 90 100
RTEEVLISDG RGSFLDRNGR ALTGQSEPAV VLFPFLLTQD WPIKKVADIL
110 120 130 140 150
GMSEDDLRQT LGQAKKPVIL QQKKIKTLSK QSITKINSLK YPGIYGVYME
160 170 180 190 200
NEDKPSLASH TIGSTNQDPA LLRKKYPDKE SLPITTEIGT TGLERTFDEF
210 220 230 240 250
LLPEQDTKLL YHVDGKGNPL FGMDVKYTAE ANTFYPLQIK TTIDQSIQKA
260 270 280 290 300
MEEVLDEQGL KKGGAVLLDI ENSSVLGIVS KPDADVSRQN TLQNYMLTPI
310 320 330 340 350
YPGSVFKTVI AAAAIENNMV KPSQTFNCNL NLYGEPGDDK GTLSFDESFA
360 370 380 390 400
QSCNYTFTSL AEQLMKKDSS VIEDMSEKLA LTDRAGWEGK LYHETDFRQL
410 420 430 440 450
YNEKSGVIWG DEKDKSVKKA IAQTAIGQKN VKVTPLEVAN MMATIARGGE
460 470 480 490 500
KRQVKIAEQI EYKNGTTLVT FKDQKLKGET IDKYTSQQLQ KILRRVVESP
510 520 530 540 550
SGTGRRFQDL PYTVAGKSGT AQTGKLSKEK ETLYEKWFAG YFPADKPKYA
560 570 580
LVVLHMDTPG DKALTNSVFY DIVKKVHEIE INQK
Length:584
Mass (Da):65,522
Last modified:January 1, 1998 - v1
Checksum:i889140C9E9D69A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB14673.1.
PIRiA69980.
RefSeqiNP_390609.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14673; CAB14673; BSU27310.
GeneIDi936016.
KEGGibsu:BSU27310.
PATRICi18977318. VBIBacSub10457_2848.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB14673.1.
PIRiA69980.
RefSeqiNP_390609.1. NC_000964.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO32032. 1 interaction.
STRINGi224308.BSU27310.

Proteomic databases

PaxDbiO32032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14673; CAB14673; BSU27310.
GeneIDi936016.
KEGGibsu:BSU27310.
PATRICi18977318. VBIBacSub10457_2848.

Organism-specific databases

GenoListiBSU27310. [Micado]

Phylogenomic databases

eggNOGiCOG0768.
HOGENOMiHOG000097173.
InParanoidiO32032.
OMAiKWFAGYF.
OrthoDBiEOG6N0HHV.
PhylomeDBiO32032.

Enzyme and pathway databases

BioCyciBSUB:BSU27310-MONOMER.

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. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "A mother cell-specific class B penicillin-binding protein, PBP4b, in Bacillus subtilis."
    Wei Y., McPherson D.C., Popham D.L.
    J. Bacteriol. 186:258-261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPBPI_BACSU
AccessioniPrimary (citable) accession number: O32032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: April 1, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.