PBPA_BACSU
ID PBPA_BACSU Reviewed; 914 AA.
AC P39793;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Penicillin-binding protein 1A/1B;
DE Short=PBP1;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=DD-transpeptidase;
GN Name=ponA; OrderedLocusNames=BSU22320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 499-515.
RC STRAIN=168;
RX PubMed=7814321; DOI=10.1128/jb.177.2.326-335.1995;
RA Popham D.L., Setlow P.;
RT "Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis
RT ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-
RT related factor.";
RL J. Bacteriol. 177:326-335(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP 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 GROWTH REQUIREMENTS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9721295; DOI=10.1128/jb.180.17.4555-4563.1998;
RA Murray T., Popham D.L., Setlow P.;
RT "Bacillus subtilis cells lacking penicillin-binding protein 1 require
RT increased levels of divalent cations for growth.";
RL J. Bacteriol. 180:4555-4563(1998).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10322023; DOI=10.1128/jb.181.10.3201-3211.1999;
RA Pedersen L.B., Angert E.R., Setlow P.;
RT "Septal localization of penicillin-binding protein 1 in Bacillus
RT subtilis.";
RL J. Bacteriol. 181:3201-3211(1999).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits) (Probable). Required for vegetative
CC growth (Probable). Has a partially redundant function with PBP-2A
CC (pbpA) during spore outgrowth (PubMed:9851991).
CC {ECO:0000269|PubMed:9851991, ECO:0000305, ECO:0000305|PubMed:3080407}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000250|UniProtKB:P02918};
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:0000250|UniProtKB:P02918};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10322023};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:10322023}.
CC Forespore inner membrane {ECO:0000269|PubMed:3080407}; Single-pass type
CC II membrane protein {ECO:0000255}. Note=Probably found all over the
CC whole cell at low concentrations. Also localizes to the division site
CC in vegetative cells.
CC -!- DEVELOPMENTAL STAGE: Expression is constant during growth, decreases
CC during sporulation and is induced approximately 15 min into spore
CC germination. Present in the inner forespore membrane of the dormant
CC spore (PubMed:3080407). {ECO:0000269|PubMed:3080407}.
CC -!- PTM: The product expressed from the translation of the ponA gene
CC appears as two bands on a gel (1A and 1B), but the specific amino acid
CC sequence of each protein is unknown.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISRUPTION PHENOTYPE: Cells require increased levels of Mg(2+) or
CC Ca(2+) for growth and germination. Approximately 50% of cells without
CC the gene contain abnormal FtsZ rings, suggesting it is involved in
CC septum synthesis; increased levels of Mg(2+) or Ca(2+) only partially
CC eliminate the septation defects (PubMed:9721295). Double ponA-pbpA
CC deletions spores have greatly decreased viability, peptidoglycan
CC synthesis and elongate poorly; increased levels of Mg(2+) increase
CC spore viability (PubMed:9851991). {ECO:0000269|PubMed:9721295,
CC ECO:0000269|PubMed:9851991}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; U11883; AAA64947.1; -; Genomic_DNA.
DR EMBL; L47838; AAB38459.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14148.1; -; Genomic_DNA.
DR PIR; I40529; I40529.
DR RefSeq; NP_390113.1; NC_000964.3.
DR RefSeq; WP_004398589.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39793; -.
DR SMR; P39793; -.
DR IntAct; P39793; 5.
DR STRING; 224308.BSU22320; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR jPOST; P39793; -.
DR PaxDb; P39793; -.
DR PRIDE; P39793; -.
DR EnsemblBacteria; CAB14148; CAB14148; BSU_22320.
DR GeneID; 939044; -.
DR KEGG; bsu:BSU22320; -.
DR PATRIC; fig|224308.179.peg.2436; -.
DR eggNOG; COG0744; Bacteria.
DR eggNOG; COG4499; Bacteria.
DR InParanoid; P39793; -.
DR OMA; LAQMAMI; -.
DR PhylomeDB; P39793; -.
DR BioCyc; BSUB:BSU22320-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase 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; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..914
FT /note="Penicillin-binding protein 1A/1B"
FT /id="PRO_0000083179"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..914
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 708..795
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..246
FT /note="Transglycosylase"
FT REGION 329..662
FT /note="Transpeptidase"
FT REGION 773..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 390
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 914 AA; 99562 MW; 6978E33DFE2423E6 CRC64;
MSDQFNSREA RRKANSKSSP SPKKGKKRKK GGLFKKTLFT LLILFVLGVV GGAVTFAVMV
SDAPSLDESK LKTPYSSTIY DKNGKEIAEV GAEKRTYVSI DEIPDVVKEA FIATEDARFY
EHHGIDPVRI GGALVANFKD GFGAEGGSTI TQQVVKNSLL SHQKTLKRKV QEVWLSIQLE
RNYSKDEILE MYLNRIYFSP RAYGIGKAAE EFFGVTDLSK LTVEQAATLA GMPQSPTAYN
PVKNPDKAEK RRNIVLSLMK KQGFISDSQY NKAKKVAVKD EGVVSQKEYE KASTNKYSAF
VEEVMKEIDE KSDVDPSADG LKIYTTLDTK AQDKLDELMD GDTVGFTEGM QGGVTLLDTK
NGEVRAIGAG RNQPVGGFNY ATQTKAQPGS TIKPILDYGP VIENKKWSTY EQIDDSAYTY
SNGKPIRDWD RKYLGPISMR YALAQSRNIP ALKAFQAVGK DTAVDFANGL GLGLTKDNVT
EAYSIGGFGG NDGVSPLTMA GAYSAFGNNG TYNEPHFVKS IEFNDGTKLD LTPKSKSAMS
DYTAFMITDM LKTAVKTGTG QLAQVPGVEV AGKTGTTNFD DNEVKRYNIA SGGARDSWFV
GYTPQYTAAV WTGMGENEAG KKSLSAEEQK VAKRIFAQLI ADVDDGSGSF EKPDSVVEAT
VEKGSNPAKL AGPNTPSDKK LTEYFVKGTA PSTVSKTYEK EEKEETAKLS GLNVKYDKDN
QSLTLSWNYD GDATFAVKQS VDGGSYSEIQ NSSAKEAVIS GVQPGSVYKF EVTAVSDDGK
STASTSYEVP KAEDDEDKKD QQQTDDEKQD DEKTQDDTQT DDSQKDDGQT DQDQTDDSTN
DQDKKQDNTN TNPSDNNNQD QSNDNDNDNS NNQDTSDGDS NSGKNDSTGS DTNKNKTDTS
NKTQTNSSSI EKTN
