PBPG_BACSU
ID PBPG_BACSU Reviewed; 691 AA.
AC P70997; Q794Z1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Penicillin-binding protein 2D;
DE Short=PBP-2D;
DE Short=PBP2d;
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=pbpG; Synonyms=ywhE; OrderedLocusNames=BSU37510;
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;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 SEQUENCE REVISION TO C-TERMINUS.
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 [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10767540; DOI=10.1016/s0378-1119(00)00084-6;
RA Pedersen L.B., Ragkousi K., Cammett T.J., Melly E., Sekowska A.,
RA Schopick E., Murray T., Setlow P.;
RT "Characterization of ywhE, which encodes a putative high-molecular-weight
RT class A penicillin-binding protein in Bacillus subtilis.";
RL Gene 246:187-196(2000).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11567005; DOI=10.1128/jb.183.20.6046-6053.2001;
RA McPherson D.C., Driks A., Popham D.L.;
RT "Two class A high-molecular-weight penicillin-binding proteins of Bacillus
RT subtilis play redundant roles in sporulation.";
RL J. Bacteriol. 183:6046-6053(2001).
CC -!- FUNCTION: Involved in the polymerization and cross-linking of spore
CC peptidoglycan. May be required for synthesis of the spore germ cell
CC wall, the first layer of peptidoglycan synthesized on the surface of
CC the inner forespore membrane. {ECO:0000269|PubMed:10767540,
CC ECO:0000269|PubMed:11567005}.
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; Single-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Sporulation specific. Expressed predominantly, if
CC not exclusively, in the forespore. {ECO:0000269|PubMed:10767540}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC PbpF. Spores have normal heat-resistance, cortex structure, and
CC germination and outgrowth properties. {ECO:0000269|PubMed:10767540,
CC ECO:0000269|PubMed:11567005}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB02515.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z80360; CAB02515.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB15778.2; -; Genomic_DNA.
DR PIR; F70057; F70057.
DR RefSeq; NP_391631.2; NC_000964.3.
DR RefSeq; WP_003227540.1; NZ_JNCM01000034.1.
DR RefSeq; WP_009968333.1; NZ_CM000487.1.
DR AlphaFoldDB; P70997; -.
DR SMR; P70997; -.
DR IntAct; P70997; 1.
DR STRING; 224308.BSU37510; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; P70997; -.
DR PRIDE; P70997; -.
DR EnsemblBacteria; CAB15778; CAB15778; BSU_37510.
DR GeneID; 937200; -.
DR KEGG; bsu:BSU37510; -.
DR PATRIC; fig|224308.179.peg.4062; -.
DR eggNOG; COG0744; Bacteria.
DR InParanoid; P70997; -.
DR OMA; YQLTSMM; -.
DR PhylomeDB; P70997; -.
DR BioCyc; BSUB:BSU37510-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 Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
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; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..691
FT /note="Penicillin-binding protein 2D"
FT /id="PRO_0000360165"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 55..223
FT /note="Transglycosylase"
FT REGION 327..605
FT /note="Transpeptidase"
FT REGION 663..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 365
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 691 AA; 77037 MW; 4E9B4CF545CF0C4A CRC64;
MDAMTNKRLR LTLKTVRAFI FLGAFAALAA AAVFMTVILI AKYQGAPSVQ VPQSTILYAS
DGSKLGETNY GEKRYWVPLK DMNPTIVKAT VAIEDQNFYD HHGFDYKRMA GAALADLKAF
AKVQGASTIT QQYARNLYLE HDKTWKRKWN EAFYTIRLEQ NYSKDEILEG YLNTIYYGHG
AYGIEAASRL YFGKHAKNLT DAEAALLAGI PKGPSGYSPY VNETKAKERQ KTIVRMMEKQ
QMISQKKADE LIKEPLSYQP LNKQVSKRKA PYFYDNAMRE LEKKLGMTRE QIETSGLNVY
TTVDKRMQRI AEETITETVN AGSDIQVGFS AIDPRTGNVL ALVGGRDYQK SPFDRTTQAK
RQPASTIKPL LYYKAIQSGF TPVTLMKSEE TEFQIDAKGE TYSPSNYNGY YANKPITLLQ
ALALSDNIYA VKTHLFLGTN KLVKTAKEFG ITAHLQALPS LALGTEPVRP IEMVNAYAML
ANGGKKIEPT FISRVTDAAG HVLYENPNQH KQVLDEKAAF VTASMMTGMF DIDLNGYTSV
TGRTIANRLT RTYAGKSGTT SADSWMIGFN PKLAAGVWTG YDKNSTIDSV EEKSYAKTIW
ADFMEDALKG EPETAFKPPK GVTGVYIDPE TGYSSGPGCA AKHYTYFVKG TEPANVCYGA
EPAKQTKDRL PSKEKPASEK KWWDKWLGRH H
