ID   PBPH_BACSU              Reviewed;         704 AA.
AC   Q796K8; O31399;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Penicillin-binding protein H;
DE            EC=3.4.16.4 {ECO:0000303|PubMed:12896990};
GN   Name=pbpH {ECO:0000303|PubMed:12896990}; Synonyms=ykuA;
GN   OrderedLocusNames=BSU13980;
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;
RA   Scanlan E., Devine K.M.;
RT   "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   FUNCTION IN CELL SHAPE DETERMINATION, TRANSLATIONAL START SITE, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PS832;
RX   PubMed=12896990; DOI=10.1128/jb.185.16.4717-4726.2003;
RA   Wei Y., Havasy T., McPherson D.C., Popham D.L.;
RT   "Rod shape determination by the Bacillus subtilis class B penicillin-
RT   binding proteins encoded by pbpA and pbpH.";
RL   J. Bacteriol. 185:4717-4726(2003).
CC   -!- FUNCTION: Involved in the polymerization of peptidoglycan. Plays a
CC       redundant role with PBP-2A (pbpA) in determining the rod shape of the
CC       cell during vegetative growth and spore outgrowth.
CC       {ECO:0000269|PubMed:12896990}.
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;
CC         Evidence={ECO:0000305|PubMed:12896990};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Increases progressively during log phase, peaking at
CC       stationary phase of vegetative growth. {ECO:0000269|PubMed:12896990}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype during vegetative growth,
CC       sporulation or spore germination. No change in antibiotic resistance.
CC       Double pbpA-pbpH mutants cannot be made, suggesting the 2 proteins have
CC       redundant, essential roles in vegetative growth. Depletion of PbpH in
CC       the pbpA deletion leads to cell growth arrest after 3 generations;
CC       cells swell, round-up, many lyse and division septa are very irregular.
CC       Germinated spore are spherical and eventually lyse.
CC       {ECO:0000269|PubMed:12896990}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-20 is the initiator; if
CC       Met-20 then the protein would probably be secreted.
CC       {ECO:0000303|PubMed:12896990}.
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DR   EMBL; AJ222587; CAA10861.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13271.2; -; Genomic_DNA.
DR   PIR; G69864; G69864.
DR   RefSeq; NP_389281.1; NC_000964.3.
DR   RefSeq; WP_003245075.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; Q796K8; -.
DR   SMR; Q796K8; -.
DR   IntAct; Q796K8; 1.
DR   STRING; 224308.BSU13980; -.
DR   PaxDb; Q796K8; -.
DR   PRIDE; Q796K8; -.
DR   EnsemblBacteria; CAB13271; CAB13271; BSU_13980.
DR   GeneID; 936204; -.
DR   KEGG; bsu:BSU13980; -.
DR   PATRIC; fig|224308.179.peg.1524; -.
DR   eggNOG; COG0768; Bacteria.
DR   OMA; TQYEMGS; -.
DR   BioCyc; BSUB:BSU13980-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: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; 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   1: Evidence at protein level;
KW   Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..704
FT                   /note="Penicillin-binding protein H"
FT                   /id="PRO_0000360660"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          197..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD65"
SQ   SEQUENCE   704 AA;  79348 MW;  623EB06EC70AA152 CRC64;
     MTEIGREPKK KSKGNRAIRM NLFFLAVFVL FTALIFKLGV VQIVEGEQHE EDAEKSNAKT
     AYYPAPRGKM YDRNQKVAVD NQSVPEIVYV STSSTKTEDK IKTAKRLASF IHIDTEFLKE
     RDLRDYWIAA HPKKAAALLK ESESNLKGDQ AYKLQIERVP DQELKAIQQD DEEMETAAIY
     TRFSSGNAYE PQIVKAMNPN KSNSNGKNGA LLDEKKNSSQ RPKNDLTYDE ISIVSEHLEE
     LPGIDIVNDW TRKYPYDKTL YSVFGGVTTP DQGLLSDRKD FYLTRGYANN DRVGKSYLEY
     QYEEYLNSHK EKVEYVEDNK GNVVSQKTID KGSRGYDLQL SFDMELQAKV EKIIEEEVRN
     SRARGNYMLD RAFAVMMDPN NGDILSMAGK KIDLKTNKIE DYAIGAFTTQ YEMGSAVKGA
     TVLAGYQDGI PHYKYYIDAP MLLGTNLIKK SYTNMGTINE LTALQKSSNV YMFNVAMHIA
     GVTYKPHGSL PADQNDLLKM RNYYSQFGLG VKTGIDLPQE SAGMQTTPKT VGGLILDLAI
     GQYDTYTPLQ MAQYISVIAN GGYRVQPRIV TSIHKPGKKD QLGKAIEHRK PKVLNKINNS
     ESDLKQVQTG MKLVTSSGTA KNTFTEDVSG KTGTAETFYY GTNRNWWGKK TYNLTFVGYY
     PSKKPKVAFS VVVPSVDDDD KINKIIAKRA IHAYAELEKK HSKK