PBPC_BACSU
ID PBPC_BACSU Reviewed; 668 AA.
AC P42971; P40772;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Penicillin-binding protein 3;
DE Short=PBP 3;
DE EC=3.4.16.4 {ECO:0000305};
DE AltName: Full=PSPB20;
DE AltName: Full=Penicillin-binding protein C;
GN Name=pbpC {ECO:0000303|PubMed:8830698}; Synonyms=ycsM, yzsA;
GN OrderedLocusNames=BSU04140;
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=8574415; DOI=10.1099/13500872-141-12-3241;
RA Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA Yamane K.;
RT "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT region of the Bacillus subtilis chromosome and similarity analysis of the
RT products of putative ORFs.";
RL Microbiology 141:3241-3245(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
RA Smith H., de Jong A., Bron S., Venema G.;
RT "Characterization of signal-sequence-coding regions selected from the
RT Bacillus subtilis chromosome.";
RL Gene 70:351-361(1988).
RN [5]
RP PROTEIN SEQUENCE OF 492-502, IDENTIFICATION OF GENE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8830698; DOI=10.1128/jb.178.20.6001-6005.1996;
RA Murray T., Popham D.L., Setlow P.;
RT "Identification and characterization of pbpC, the gene encoding Bacillus
RT subtilis penicillin-binding protein 3.";
RL J. Bacteriol. 178:6001-6005(1996).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-410, 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 (Probable). Probably required for both cortical
CC and vegetative peptidoglycan synthesis (Probable). Although not usually
CC required for cell division, in the absence of PBP 2B (pbpB) it becomes
CC essential. Confers resistance to oxacillin and cephalexin
CC (PubMed:28792086). {ECO:0000269|PubMed:28792086, ECO:0000305,
CC ECO:0000305|PubMed:3080407}.
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:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:3080407}; Single-pass
CC membrane protein {ECO:0000305}. Forespore inner membrane
CC {ECO:0000269|PubMed:3080407}; Single-pass membrane protein
CC {ECO:0000255}. Forespore outer membrane {ECO:0000269|PubMed:3080407};
CC Single-pass membrane protein. Membrane raft
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Single-pass
CC membrane protein {ECO:0000255}. Note=Localizes at mid cell;
CC localization requires FtsZ and PBP 2B (pbpB) (PubMed:28792086). Present
CC in detergent-resistant membrane (DRM) fractions that may be equivalent
CC to eukaryotic membrane rafts; these rafts include proteins involved in
CC signaling, molecule trafficking and protein secretion (PubMed:20713508,
CC PubMed:22882210). {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:28792086}.
CC -!- DEVELOPMENTAL STAGE: Present in all growth stages and in both inner and
CC outer forespore membranes. {ECO:0000269|PubMed:3080407}.
CC -!- INDUCTION: Transcribed during vegetative growth, drops off after entry
CC into stationary phase and the onset of sporulation. Transcription rises
CC again 70-80 minutes after germination. {ECO:0000269|PubMed:8830698}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in growth, sporulation,
CC spore germination, outgrowth, or spore heat resistance
CC (PubMed:8830698). No visible phenotype in the absence of antibiotics;
CC loss of resistance to oxacillin and cephalexin but not penicillin G. It
CC cannot be deleted in the absence of a catalytically inactive copy of
CC penicillin-binding protein 2B (pbpB) (PubMed:28792086).
CC {ECO:0000269|PubMed:28792086, ECO:0000269|PubMed:8830698}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR EMBL; D38161; BAA07365.1; -; Genomic_DNA.
DR EMBL; D50453; BAA09043.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12221.1; -; Genomic_DNA.
DR EMBL; M22913; AAA22829.1; -; Genomic_DNA.
DR PIR; I39902; I39902.
DR RefSeq; NP_388295.1; NC_000964.3.
DR RefSeq; WP_003246590.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P42971; -.
DR SMR; P42971; -.
DR IntAct; P42971; 1.
DR STRING; 224308.BSU04140; -.
DR BindingDB; P42971; -.
DR ChEMBL; CHEMBL3112383; -.
DR DrugBank; DB00355; Aztreonam.
DR DrugBank; DB00493; Cefotaxime.
DR DrugBank; DB01598; Imipenem.
DR DrugBank; DB04570; Latamoxef.
DR DrugCentral; P42971; -.
DR jPOST; P42971; -.
DR PaxDb; P42971; -.
DR PRIDE; P42971; -.
DR EnsemblBacteria; CAB12221; CAB12221; BSU_04140.
DR GeneID; 940139; -.
DR KEGG; bsu:BSU04140; -.
DR PATRIC; fig|224308.179.peg.440; -.
DR eggNOG; COG0768; Bacteria.
DR InParanoid; P42971; -.
DR OMA; GPVPFKV; -.
DR PhylomeDB; P42971; -.
DR BioCyc; BSUB:BSU04140-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P42971; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF54427; SSF54427; 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..668
FT /note="Penicillin-binding protein 3"
FT /id="PRO_0000195464"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 410
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
FT MUTAGEN 410
FT /note="S->A: Required for cell division in the presence of
FT a transpeptidase-inactive copy of PBP-2B. Loss of oxacillin
FT and cephalexin resistance."
FT /evidence="ECO:0000269|PubMed:28792086"
FT CONFLICT 9
FT /note="V -> D (in Ref. 4; AAA22829)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..37
FT /note="RMEAFVKQ -> PLESTAQA (in Ref. 4; AAA22829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 74406 MW; A877A27B188ECAFC CRC64;
MLKKCILLVF LCVGLIGLIG CSKTDSPEDR MEAFVKQWND QQFDDMYQSL TKDVKKEISK
KDFVNRYKAI YEQAGVKNLK VTAGEVDKDD QDNKTMKHIP YKVSMNTNAG KVSFKNTAVL
KLEKTDDEES WNIDWDPSFI FKQLADDKTV QIMSIEPKRG QIYDKNGKGL AVNTDVPEIG
IVPGELGDKK EKVIKELAKK LDLTEDDIKK KLDQGWVKDD SFVPLKKVKP DQEKLVSEAT
SLQGVTRTNV SSRYYPYGEK TAHLTGYVRA ITAEELKKKK EGTYSDTSNI GIAGLENVYE
DKLRGTTGWK IYVPQTGEVI AEKKAKDGED LHLTIDIKTQ MKLYDELKDD SGAAVALQPK
TGETLALVSA PSYDPNGFIF GWSDKEWKKL NKDKNNPFSA KFNKTYAPGS TIKPIAAAIG
IKNGTLKADE KKTIKGKEWQ KDSSWGGYSV TRVSERLQQV DLENALITSD NIYFAQNALD
MGADTFTKGL KTFGFSEDVP YEFPIQKSSI ANDKLDSDIL LADTGYGQGQ MQMSPLHLAT
AYTPFVDNGD LVKPTLIKKD SQTADVWHKQ VVTKEGAADI TKGLKGVVED ERGSAYQPVV
KGITVAGKTG TAELKTSKDD KDGTENGWFV GYDYENKDLL VAMMIQNVQD RGGSHYVVEK
AKKQFQSN
