PBP2B_BACSU
ID PBP2B_BACSU Reviewed; 713 AA.
AC Q07868;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Penicillin-binding protein 2B {ECO:0000303|PubMed:8244929};
DE Short=PBP-2B;
DE EC=3.4.16.4 {ECO:0000305|PubMed:28792086};
DE AltName: Full=Penicillin-binding protein B;
DE AltName: Full=Penicillin-sensitive peptidoglycan D,D-transpeptidase {ECO:0000305};
GN Name=pbpB {ECO:0000303|PubMed:8244929}; OrderedLocusNames=BSU15160;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF 630-ALA--ASP-713, AND PENICILLIN-BINDING.
RC STRAIN=168;
RX PubMed=8244929; DOI=10.1128/jb.175.23.7604-7616.1993;
RA Yanouri A., Daniel R.A., Errington J., Buchanan C.E.;
RT "Cloning and sequencing of the cell division gene pbpB, which encodes
RT penicillin-binding protein 2B in Bacillus subtilis.";
RL J. Bacteriol. 175:7604-7616(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8636036; DOI=10.1128/jb.178.8.2343-2350.1996;
RA Daniel R.A., Williams A.M., Errington J.;
RT "A complex four-gene operon containing essential cell division gene pbpB in
RT Bacillus subtilis.";
RL J. Bacteriol. 178:2343-2350(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 147.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 674-713.
RC STRAIN=168;
RX PubMed=8289242; DOI=10.1016/s0022-2836(05)80027-0;
RA Daniel R.A., Drake S., Buchanan C.E., Scholle R., Errington J.;
RT "The Bacillus subtilis spoVD gene encodes a mother-cell-specific
RT penicillin-binding protein required for spore morphogenesis.";
RL J. Mol. Biol. 235:209-220(1994).
RN [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PENICILLIN-BINDING.
RC STRAIN=168;
RX PubMed=3080407; DOI=10.1128/jb.165.2.498-503.1986;
RA Buchanan C.E., Neyman S.L.;
RT "Correlation of penicillin-binding protein composition with different
RT functions of two membranes in Bacillus subtilis forespores.";
RL J. Bacteriol. 165:498-503(1986).
RN [7]
RP DEPLETION EXPERIMENTS.
RC STRAIN=168;
RX PubMed=16936019; DOI=10.1128/jb.01031-06;
RA Daniel R.A., Noirot-Gros M.F., Noirot P., Errington J.;
RT "Multiple interactions between the transmembrane division proteins of
RT Bacillus subtilis and the role of FtsL instability in divisome assembly.";
RL J. Bacteriol. 188:7396-7404(2006).
RN [8]
RP SUBCELLULAR LOCATION, DEPLETION, MUTAGENESIS OF SER-309, AND
RP PENICILLIN-BINDING.
RC STRAIN=168;
RX PubMed=28792086; DOI=10.1111/mmi.13765;
RA Sassine J., Xu M., Sidiq K.R., Emmins R., Errington J., Daniel R.A.;
RT "Functional redundancy of division specific penicillin-binding proteins in
RT Bacillus subtilis.";
RL Mol. Microbiol. 106:304-318(2017).
CC -!- FUNCTION: Penicillin-binding proteins (PBPs) function in the late steps
CC of murein biosynthesis. PBP-2B is required for vegetative cell division
CC and sporulation septation. Beta-lactamase inactivates the PBPs by
CC acylating an essential serine residue in the active site of these
CC proteins, thereby interrupting normal cell wall synthesis (Probable).
CC This protein itself, but not its transpeptidase activity, is required
CC for cell division (PubMed:28792086). {ECO:0000269|PubMed:28792086,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000305|PubMed:28792086};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- INTERACTION:
CC Q07868; P16655: divIB; NbExp=3; IntAct=EBI-5243272, EBI-5243256;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3080407,
CC ECO:0000269|PubMed:8244929, ECO:0000305|PubMed:28792086}; Single-pass
CC membrane protein {ECO:0000255}. Note=Localizes at mid cell, to cell
CC division sites; localization requires FtsZ.
CC {ECO:0000269|PubMed:28792086}.
CC -!- DEVELOPMENTAL STAGE: Synthesized throughout vegetative growth.
CC Synthesis is enhanced during stage II of sporulation and in stage IV
CC mother cells. Undetectable in stage IV forespores. Present in the inner
CC forespore membrane of the dormant spore. {ECO:0000269|PubMed:3080407}.
CC -!- INDUCTION: Transcribed at a low constant level in all growth phases.
CC Part of the mraZ-rsmH-ftsL-pbpB operon. {ECO:0000269|PubMed:8636036}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted (PubMed:8244929,
CC PubMed:8636036). Depletion leads to an arrest of cell division after 80
CC minutes at 37 degrees Celsius and 40 minutes at 48 degrees Celsius with
CC a concomitant reduction in FtsL and to a lesser extent DivIC levels;
CC cells lengthen after arrest and eventually lyse (PubMed:16936019,
CC PubMed:28792086). {ECO:0000269|PubMed:16936019,
CC ECO:0000269|PubMed:28792086, ECO:0000269|PubMed:8244929,
CC ECO:0000269|PubMed:8636036}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36837.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA81084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA92527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB13389.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L09703; AAC36837.1; ALT_INIT; Unassigned_DNA.
DR EMBL; Z68230; CAA92527.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13389.2; ALT_INIT; Genomic_DNA.
DR EMBL; Z25865; CAA81084.1; ALT_INIT; Genomic_DNA.
DR PIR; C53292; C53292.
DR RefSeq; NP_389399.2; NC_000964.3.
DR AlphaFoldDB; Q07868; -.
DR SMR; Q07868; -.
DR IntAct; Q07868; 14.
DR STRING; 224308.BSU15160; -.
DR PaxDb; Q07868; -.
DR PRIDE; Q07868; -.
DR EnsemblBacteria; CAB13389; CAB13389; BSU_15160.
DR GeneID; 939847; -.
DR KEGG; bsu:BSU15160; -.
DR PATRIC; fig|224308.43.peg.1610; -.
DR eggNOG; COG0768; Bacteria.
DR InParanoid; Q07868; -.
DR PhylomeDB; Q07868; -.
DR BioCyc; BSUB:BSU15160-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03793; PASTA; 2.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS51178; PASTA; 2.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carboxypeptidase; Cell cycle; Cell division;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Repeat;
KW Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..713
FT /note="Penicillin-binding protein 2B"
FT /id="PRO_0000195463"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:8244929"
FT TRANSMEM 11..28
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:8244929"
FT TOPO_DOM 29..309
FT /note="Extracellular"
FT /evidence="ECO:0000303|PubMed:8244929"
FT DOMAIN 595..654
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 655..711
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT ACT_SITE 309
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65,
FT ECO:0000303|PubMed:8244929"
FT MUTAGEN 309
FT /note="S->A: Bacteria grow as well as wild-type, are
FT slightly longer, protein no longer binds bocillin-FL (a
FT penicillin analog). Increased sensitivity to cefoxitin,
FT very slight increase in resistance to penicillin G and
FT cephalexin."
FT /evidence="ECO:0000269|PubMed:28792086"
FT MUTAGEN 630..713
FT /note="AVKEQYPKADEEVLTNQKVFLKTGGKIKMPDMTGWSRREVLQYGELAGIHIE
FT VSGQGYAVSQSVKKDKEIKDKTVIKVKFKNPD->SFCSL: Cells are viable
FT and motile, however they are filamentous and only about 20%
FT of cells produce spores. Less protein is made, still binds
FT penicillin."
FT /evidence="ECO:0000269|PubMed:8244929"
FT CONFLICT 147
FT /note="Q -> L (in Ref. 1; AAC36837 and 2; CAA92527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 78948 MW; B173ABEF5F1C944C CRC64;
MPKKNKFMNR GAAILSICFA LFFFVILGRM AYIQITGKAN GEVLATKATE QHEKKRTIEA
SRGSILDRKG KVIAEDTATY KLIAILDKKM TTDVKHPQHV VNKEKTAEAL SKVINLDKAD
ILDILNKDAK QVEFGSAGRD ITYSQKQKIE KMKLPGISFL RDTKRYYPNG VFASNLIGYA
EVDEETNEIS GAMGLEKVLD KYLKERDGYV TYESDKSGWE LPNSKNKITA PKNGDNVYLT
IDQKIQTFLE DSMTKVAQKY NPKKIMAAVV DPKTGKVLAM GQRPSFDPNK RDVTNYYNDL
ISYAYEPGST MKIFTLAAAM QENVFNANEK YKSGTFEVGG APVKDHNNGV GWGPTTYHDG
VLRSSNVAFA KLAKEKLGYD RLNQYLHKFN FYQKTGIDLP GEVSSKINFK YEFDKASTAY
GQASAVTPIQ QIQAATAIAN DGKMMKPYVI DHIVDPDKDK TIYQNKPESA GTPISASTAK
KVRDILGEVV TSKIGTGQAY KIEGFDVAGK TGTAQIAGKG GYLDGTDNYI FSFMGMAPKD
DPELLIYVAV QQPQLKAGQS SSDPVSEIFN PTMKNSLHYL NIEPTEKSDS DKEETKAQTM
PDLTDQTVAA AQKKAKEENL TPIVIGSDVA VKEQYPKADE EVLTNQKVFL KTGGKIKMPD
MTGWSRREVL QYGELAGIHI EVSGQGYAVS QSVKKDKEIK DKTVIKVKFK NPD
