PBP2A_BACSU
ID PBP2A_BACSU Reviewed; 716 AA.
AC P54488;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Penicillin-binding protein 2A {ECO:0000303|PubMed:3080407};
DE Short=PBP-2B;
DE EC=3.4.16.4 {ECO:0000305};
GN Name=pbpA {ECO:0000303|PubMed:9139922}; Synonyms=yqgF;
GN OrderedLocusNames=BSU25000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 241-264 AND 401-426, IDENTIFICATION OF GENE, FUNCTION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9139922; DOI=10.1128/jb.179.9.3021-3029.1997;
RA Murray T., Popham D.L., Setlow P.;
RT "Identification and characterization of pbpA encoding Bacillus subtilis
RT penicillin-binding protein 2A.";
RL J. Bacteriol. 179:3021-3029(1997).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PS832;
RX PubMed=9851991; DOI=10.1128/jb.180.24.6493-6502.1998;
RA Murray T., Popham D.L., Pearson C.B., Hand A.R., Setlow P.;
RT "Analysis of outgrowth of Bacillus subtilis spores lacking penicillin-
RT binding protein 2a.";
RL J. Bacteriol. 180:6493-6502(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PS832;
RX PubMed=12896990; DOI=10.1128/jb.185.16.4717-4726.2003;
RA Wei Y., Havasy T., McPherson D.C., Popham D.L.;
RT "Rod shape determination by the Bacillus subtilis class B penicillin-
RT binding proteins encoded by pbpA and pbpH.";
RL J. Bacteriol. 185:4717-4726(2003).
CC -!- FUNCTION: Involved in the synthesis of peptidoglycan associated with
CC cell wall elongation, especially following spore germination
CC (PubMed:9139922). Has a partially redundant function with PBP 1 (ponA)
CC or PBP 4 (pbpD) during spore outgrowth (PubMed:9851991). Plays a
CC redundant role with PbpH in determining the rod shape of the cell
CC during vegetative growth and spore outgrowth (PubMed:12896990).
CC {ECO:0000269|PubMed:12896990, ECO:0000269|PubMed:9139922,
CC ECO:0000269|PubMed:9851991}.
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; Evidence={ECO:0000305};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3080407}.
CC Forespore inner membrane {ECO:0000269|PubMed:3080407}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells. Also present in
CC dormant spores in the forespore inner membrane.
CC {ECO:0000269|PubMed:3080407}.
CC -!- INDUCTION: Transcribed during vegetative phase, drops off during
CC sporulation, rises again 30-40 minutes after germination. A small
CC amount is present in dormant spores. {ECO:0000269|PubMed:9139922}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype during vegetative growth
CC rate in rich media, no difference in sporulation or initial spore
CC germination. Spores have a significant delay in outgrowth, between 60-
CC 90 minutes cells swell rather than elongate, upon eventual elongation
CC they have a larger diameter and are often bent (PubMed:9139922,
CC PubMed:9851991). Single deletions have reduced peptidoglycan (PG)
CC synthesis and turnover rates. Double ponA-pbpA deletions spores have
CC greatly decreased viability, PG synthesis and elongate poorly;
CC increased levels of Mg(2+) increase spore viability. Double pbpA-pbpD
CC deletions spores have greatly decreased spore outgrowth and
CC peptidoglycan synthesis (PubMed:9851991). Single pbpA mutants are less
CC resistant to ceftriaxone and mecillinam. Double pbpA-pbpH mutants
CC cannot be made, suggesting the 2 proteins have redundant, essential
CC roles in vegetative growth (PubMed:12896990).
CC {ECO:0000269|PubMed:12896990, ECO:0000269|PubMed:9139922,
CC ECO:0000269|PubMed:9851991}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84432; BAA12509.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14430.1; -; Genomic_DNA.
DR PIR; E69672; E69672.
DR RefSeq; NP_390379.1; NC_000964.3.
DR RefSeq; WP_004398702.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54488; -.
DR SMR; P54488; -.
DR STRING; 224308.BSU25000; -.
DR MEROPS; X52.001; -.
DR PaxDb; P54488; -.
DR PRIDE; P54488; -.
DR EnsemblBacteria; CAB14430; CAB14430; BSU_25000.
DR GeneID; 938199; -.
DR KEGG; bsu:BSU25000; -.
DR PATRIC; fig|224308.179.peg.2719; -.
DR eggNOG; COG0768; Bacteria.
DR OMA; REIMDAY; -.
DR PhylomeDB; P54488; -.
DR BioCyc; BSUB:BSU25000-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:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..716
FT /note="Penicillin-binding protein 2A"
FT /id="PRO_0000195473"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 689..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
SQ SEQUENCE 716 AA; 80142 MW; A8F4A4C498D6AD0F CRC64;
MRRNKPKKQN HKEKKKSLPI RLNILFLAAF VIFTWIIVEL GIKQIVQGDD YKNQANKQEQ
SEVSSAVPRG KIYDRNFNAI VTNKALNAIT YTRSKSTTQE QRLKIAKKLS DMIKVDTKKV
TERDKKDYWI LTRPKEAKKL ISSKERQQVE DKKISDDDLY QLQLKRITDK QLNELTDKDM
QILAIKRQMD SGYALTPQYI KNEDVSAKEM AVVSEHLDEL PGVDVTSDWE REYPYKNLLR
SVLGSVSSSN EGLPSNLLDH YLSLGYSRND RVGKSYLEYQ YESLLQGQKA KVENITDSKG
NVTGTKTVSE GKAGKDLVLT IDIDLQKSVE KIIEKKLKAA KARPSTELLD RAFVVMMDPR
NGEVLTMAGK QIKRENGAYK FDDYALGAMT SSYAMGSAVK GATVLTGLQT GAINLNTVFK
DEPLYIGQDK RGKKSWQNLG PVGIQTALEK SSNVFMFKTA IAVGKGEYKP HQALPLDTSA
FDTFRNYFSQ FGLGVKTGID LPNEMTGYKG TSRLSGFLLD FAIGQYDTYT PLELAQYVST
IANGGYRMKP QLVKEVRDSN AKKGIGAVVD SVQPEVLNKV DMKSSYIEEV QAGFRRVATK
GTAAGQLASA SYKPAAKTGT AQSFYDGPDK SKTGTDTYNT TLVAYAPADN PEIAISVVVP
WTYIDYNQRY SITNEIGREV MDKYFELKSK QDKEGTQQKN KDKIEENAEN TTSSDN
