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   27-MAR-2024, entry version 147.
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; Bacillota; 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 /
RC   NCIMB 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 /
RC   NCIMB 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; 224308-BSU04140; -.
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   OrthoDB; 9766847at2; -.
DR   PhylomeDB; P42971; -.
DR   BioCyc; BSUB:BSU04140-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:P42971; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 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   PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 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
//