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O32032

- PBPI_BACSU

UniProt

O32032 - PBPI_BACSU

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Protein

Penicillin-binding protein 4B

Gene

pbpI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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: 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-KW
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.

Structurei

3D structure databases

ProteinModelPortaliO32032.
ModBaseiSearch...
MobiDBiSearch...

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 .
PIRi A69980.
RefSeqi NP_390609.1. NC_000964.3.

3D structure databases

ProteinModelPortali O32032.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O32032. 1 interaction.
STRINGi 224308.BSU27310.

Proteomic databases

PaxDbi O32032.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14673 ; CAB14673 ; BSU27310 .
GeneIDi 936016.
KEGGi bsu:BSU27310.
PATRICi 18977318. VBIBacSub10457_2848.

Organism-specific databases

GenoListi BSU27310. [Micado ]

Phylogenomic databases

eggNOGi COG0768.
HOGENOMi HOG000097173.
InParanoidi O32032.
OMAi KWFAGYF.
OrthoDBi EOG6N0HHV.
PhylomeDBi O32032.

Enzyme and pathway databases

BioCyci BSUB:BSU27310-MONOMER.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view ]
Pfami PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view ]
SUPFAMi SSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 2 hits.
ProtoNeti Search...

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(1997) [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(2004) [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: October 29, 2014
This is version 82 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