ID   PBPI_BACSU              Reviewed;         584 AA.
AC   O32032;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Penicillin-binding protein 4B;
DE            Short=PBP-4B;
DE            Short=PBP4b;
DE            EC=3.4.16.4 {ECO:0000305};
DE   AltName: Full=Penicillin-binding protein I;
GN   Name=pbpI; Synonyms=yrrR; OrderedLocusNames=BSU27310;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PS832;
RX   PubMed=14679248; DOI=10.1128/jb.186.1.258-261.2004;
RA   Wei Y., McPherson D.C., Popham D.L.;
RT   "A mother cell-specific class B penicillin-binding protein, PBP4b, in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 186:258-261(2004).
CC   -!- FUNCTION: Penicillin-binding protein with an unknown catalytic
CC       activity. Penicillin-binding proteins (PBPs) function in the late steps
CC       of murein biosynthesis. Beta-lactamase inactivates the PBPs by
CC       acylating an essential serine residue in the active site of these
CC       proteins, thereby interrupting normal cell wall synthesis.
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:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Sporulation specific. Expression starts 1 to 2
CC       hours after the initiation of sporulation. Found only in mother cells.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Spores have normal
CC       morphology, heat-resistance, cortex structure, and germination and
CC       outgrowth properties. {ECO:0000269|PubMed:14679248}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB14673.1; -; Genomic_DNA.
DR   PIR; A69980; A69980.
DR   RefSeq; NP_390609.1; NC_000964.3.
DR   RefSeq; WP_004398903.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O32032; -.
DR   SMR; O32032; -.
DR   BioGRID; 853710; 2.
DR   IntAct; O32032; 1.
DR   STRING; 224308.BSU27310; -.
DR   PaxDb; O32032; -.
DR   PRIDE; O32032; -.
DR   EnsemblBacteria; CAB14673; CAB14673; BSU_27310.
DR   GeneID; 936016; -.
DR   KEGG; bsu:BSU27310; -.
DR   PATRIC; fig|224308.179.peg.2967; -.
DR   eggNOG; COG0768; Bacteria.
DR   InParanoid; O32032; -.
DR   OMA; KWFAGYF; -.
DR   PhylomeDB; O32032; -.
DR   BioCyc; BSUB:BSU27310-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cell cycle; Cell division; Cell membrane; Hydrolase;
KW   Membrane; Protease; Reference proteome; Signal-anchor; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..584
FT                   /note="Penicillin-binding protein 4B"
FT                   /id="PRO_0000360667"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..584
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        304
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
SQ   SEQUENCE   584 AA;  65522 MW;  889140C9E9D69A13 CRC64;
     MKISKRMKLA VIAFLIVFFL LLLRLAEIQL FFTESFSKKK INLIQESVKQ RTEEVLISDG
     RGSFLDRNGR ALTGQSEPAV VLFPFLLTQD WPIKKVADIL GMSEDDLRQT LGQAKKPVIL
     QQKKIKTLSK QSITKINSLK YPGIYGVYME NEDKPSLASH TIGSTNQDPA LLRKKYPDKE
     SLPITTEIGT TGLERTFDEF LLPEQDTKLL YHVDGKGNPL FGMDVKYTAE ANTFYPLQIK
     TTIDQSIQKA MEEVLDEQGL KKGGAVLLDI ENSSVLGIVS KPDADVSRQN TLQNYMLTPI
     YPGSVFKTVI AAAAIENNMV KPSQTFNCNL NLYGEPGDDK GTLSFDESFA QSCNYTFTSL
     AEQLMKKDSS VIEDMSEKLA LTDRAGWEGK LYHETDFRQL YNEKSGVIWG DEKDKSVKKA
     IAQTAIGQKN VKVTPLEVAN MMATIARGGE KRQVKIAEQI EYKNGTTLVT FKDQKLKGET
     IDKYTSQQLQ KILRRVVESP SGTGRRFQDL PYTVAGKSGT AQTGKLSKEK ETLYEKWFAG
     YFPADKPKYA LVVLHMDTPG DKALTNSVFY DIVKKVHEIE INQK