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O32032 (PBPI_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penicillin-binding protein 4B

Short name=PBP-4B
Short name=PBP4b
Alternative name(s):
Penicillin-binding protein I
Gene names
Name:pbpI
Synonyms:yrrR
Ordered Locus Names:BSU27310
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subcellular location

Cell membrane; Single-pass type II membrane protein Potential.

Developmental stage

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

Disruption phenotype

No visible phenotype. Spores have normal morphology, heat-resistance, cortex structure, and germination and outgrowth properties. Ref.2

Sequence similarities

Belongs to the transpeptidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 584584Penicillin-binding protein 4B
PRO_0000360667

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 584552Extracellular Potential

Sites

Active site3041Acyl-ester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O32032 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 889140C9E9D69A13

FASTA58465,522
        10         20         30         40         50         60 
MKISKRMKLA VIAFLIVFFL LLLRLAEIQL FFTESFSKKK INLIQESVKQ RTEEVLISDG 

        70         80         90        100        110        120 
RGSFLDRNGR ALTGQSEPAV VLFPFLLTQD WPIKKVADIL GMSEDDLRQT LGQAKKPVIL 

       130        140        150        160        170        180 
QQKKIKTLSK QSITKINSLK YPGIYGVYME NEDKPSLASH TIGSTNQDPA LLRKKYPDKE 

       190        200        210        220        230        240 
SLPITTEIGT TGLERTFDEF LLPEQDTKLL YHVDGKGNPL FGMDVKYTAE ANTFYPLQIK 

       250        260        270        280        290        300 
TTIDQSIQKA MEEVLDEQGL KKGGAVLLDI ENSSVLGIVS KPDADVSRQN TLQNYMLTPI 

       310        320        330        340        350        360 
YPGSVFKTVI AAAAIENNMV KPSQTFNCNL NLYGEPGDDK GTLSFDESFA QSCNYTFTSL 

       370        380        390        400        410        420 
AEQLMKKDSS VIEDMSEKLA LTDRAGWEGK LYHETDFRQL YNEKSGVIWG DEKDKSVKKA 

       430        440        450        460        470        480 
IAQTAIGQKN VKVTPLEVAN MMATIARGGE KRQVKIAEQI EYKNGTTLVT FKDQKLKGET 

       490        500        510        520        530        540 
IDKYTSQQLQ KILRRVVESP SGTGRRFQDL PYTVAGKSGT AQTGKLSKEK ETLYEKWFAG 

       550        560        570        580 
YFPADKPKYA LVVLHMDTPG DKALTNSVFY DIVKKVHEIE INQK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB14673.1.
PIRA69980.
RefSeqNP_390609.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32032.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO32032. 1 interaction.
STRING224308.BSU27310.

Proteomic databases

PaxDbO32032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14673; CAB14673; BSU27310.
GeneID936016.
KEGGbsu:BSU27310.
PATRIC18977318. VBIBacSub10457_2848.

Organism-specific databases

GenoListBSU27310. [Micado]

Phylogenomic databases

eggNOGCOG0768.
HOGENOMHOG000097173.
OMAKWFAGYF.
OrthoDBEOG6N0HHV.
ProtClustDBCLSK887662.

Enzyme and pathway databases

BioCycBSUB:BSU27310-MONOMER.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 2 hits.
ProtoNetSearch...

Entry information

Entry namePBPI_BACSU
AccessionPrimary (citable) accession number: O32032
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList