ID   PBPE_BACSU              Reviewed;         451 AA.
AC   P32959;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Penicillin-binding protein 4*;
DE            Short=PBP 4*;
DE   AltName: Full=PBP 4A;
DE   AltName: Full=Penicillin-binding protein E;
GN   Name=pbpE; OrderedLocusNames=BSU34440;
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 1-14.
RX   PubMed=8491712; DOI=10.1128/jb.175.10.2917-2925.1993;
RA   Popham D.L., Setlow P.L.;
RT   "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE
RT   operon, which codes for penicillin-binding protein 4* and an apparent amino
RT   acid racemase.";
RL   J. Bacteriol. 175:2917-2925(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Denizot F.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND 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).
CC   -!- FUNCTION: Probably involved in peptidoglycan modification during cortex
CC       synthesis.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Forespore outer membrane
CC       {ECO:0000269|PubMed:3080407}; Peripheral membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed during sporulation. Detected in mature
CC       spores (PubMed:3080407). {ECO:0000269|PubMed:3080407}.
CC   -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB08016.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L10629; AAA22640.1; -; Genomic_DNA.
DR   EMBL; Z94043; CAB08016.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB15449.1; -; Genomic_DNA.
DR   PIR; A36908; A36908.
DR   RefSeq; NP_391324.1; NC_000964.3.
DR   RefSeq; WP_003243737.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P32959; -.
DR   SMR; P32959; -.
DR   STRING; 224308.BSU34440; -.
DR   PaxDb; P32959; -.
DR   EnsemblBacteria; CAB15449; CAB15449; BSU_34440.
DR   GeneID; 938615; -.
DR   KEGG; bsu:BSU34440; -.
DR   PATRIC; fig|224308.179.peg.3731; -.
DR   eggNOG; COG1680; Bacteria.
DR   InParanoid; P32959; -.
DR   OMA; WIGHNGS; -.
DR   PhylomeDB; P32959; -.
DR   BioCyc; BSUB:BSU34440-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR021860; Peptidase_S12_Pab87-rel_C.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF11954; DUF3471; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Membrane; Peptidoglycan synthesis; Reference proteome;
KW   Sporulation.
FT   CHAIN           1..451
FT                   /note="Penicillin-binding protein 4*"
FT                   /id="PRO_0000195465"
FT   ACT_SITE        61
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   451 AA;  51437 MW;  38AE2A4985DFFED7 CRC64;
     MKQNKRKHLQ TLFETLGEKH QFNGTVLAAE GGDILYHHSF GYAEMTEKRP LKTNSLFELA
     SLSKPFTALG IILLEEKGIL GYEDKVDRWL PGFPYQGVTI RHLLNHTSGL PDYMGWFFAN
     WDSHKIAVNQ DIVDMLMNEG LSGYFEPNEG WMYSNTGYVL LAVIIEKASG MSYADFIKTS
     IFLPAGMNET RVYNRRLSPE RIDHYAYGYV YDVHSETYVL PDELEETNYV VYLDGIQGDG
     TVNSVTSDLF RFDQALYQDD FISKASKESA FSPVRLNNGE TIDYGFGWVL QNSPEKGRIV
     SHSGGWPGYS TMMIRYIDHR KTLIYLSNKE EDTEYEQAIL KAAEHILFGQ PYDVPERPAD
     KKKKAIDTAI YSRYVGSYLL QDGTAAQVTT ENERLYLEIA GQLRLELFPS SETRFFLRAL
     SVEVEFTLGE DAAKSFILYE DGSEEEAVRT K