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 02-SEP-2026, entry version 154. 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; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC 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}. 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; 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; NC_000964.3. DR PDB; 7BN9; X-ray; 2.65 A; A/B=29-668. DR AlphaFoldDB; P42971; -. DR SMR; P42971; -. DR FunCoup; P42971; 29. 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 AbasyAtlas; P42971; -. DR GO; GO:0045121; C:membrane raft; EXP:UniProtKB. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. 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:0046677; P:response to antibiotic; IEA:InterPro. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR Gene3D; 3.10.450.100; NTF2-like, domain 1; 1. DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1. DR Gene3D; 3.30.1390.30; Penicillin-binding protein 2a, domain 3; 1. DR InterPro; IPR050515; Beta-lactam/transpept. 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. DR PDBsum; 7BN9; -. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Carboxypeptidase; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing; KW Hydrolase; 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" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 43..47 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 60..74 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 96..107 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 110..125 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 169..181 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 183..189 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 190..201 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 205..212 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 233..240 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 245..254 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 273..278 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 300..304 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 337..347 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 350..358 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 359..362 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 363..371 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 377..380 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 384..392 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 413..422 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 436..439 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 443..447 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 458..460 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 462..467 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 471..481 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 483..492 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 493..496 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 518..526 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 535..541 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 543..545 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 566..568 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 574..589 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 605..613 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 625..633 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 634..636 FT /evidence="ECO:0007829|PDB:7BN9" FT STRAND 640..646 FT /evidence="ECO:0007829|PDB:7BN9" FT TURN 649..653 FT /evidence="ECO:0007829|PDB:7BN9" FT HELIX 654..662 FT /evidence="ECO:0007829|PDB:7BN9" 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 //