PBPF_BACSU
ID PBPF_BACSU Reviewed; 714 AA.
AC P38050;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Penicillin-binding protein 1F;
DE Short=PBP-1F;
DE AltName: Full=Penicillin-binding protein F;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=DD-transpeptidase;
GN Name=pbpF; Synonyms=ponA; OrderedLocusNames=BSU10110;
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;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 SEQUENCE REVISION TO 120.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RC STRAIN=168;
RX PubMed=8335642; DOI=10.1128/jb.175.15.4870-4876.1993;
RA Popham D.L., Setlow P.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF
RT gene, which codes for a putative class A high-molecular-weight penicillin-
RT binding protein.";
RL J. Bacteriol. 175:4870-4876(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-714.
RX PubMed=1459957; DOI=10.1128/jb.174.24.8081-8093.1992;
RA Hansson M., Hederstedt L.;
RT "Cloning and characterization of the Bacillus subtilis hemEHY gene cluster,
RT which encodes protoheme IX biosynthetic enzymes.";
RL J. Bacteriol. 174:8081-8093(1992).
CC -!- FUNCTION: Cell wall formation. May be involved in outgrowth of the
CC germinated spore or it could function in the synthesis of the germ cell
CC wall.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000250|UniProtKB:P02918};
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:0000250|UniProtKB:P02918};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expression remains constant during vegetative
CC growth, decreases during early sporulation, and is induced in the
CC forespore during late sporulation.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; Y14083; CAA74517.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12851.2; -; Genomic_DNA.
DR EMBL; L10630; AAA71942.1; -; Genomic_DNA.
DR EMBL; M97208; AAA22516.1; -; Genomic_DNA.
DR PIR; A40614; A40614.
DR RefSeq; NP_388892.2; NC_000964.3.
DR RefSeq; WP_003233213.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P38050; -.
DR SMR; P38050; -.
DR IntAct; P38050; 1.
DR STRING; 224308.BSU10110; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; P38050; -.
DR PRIDE; P38050; -.
DR EnsemblBacteria; CAB12851; CAB12851; BSU_10110.
DR GeneID; 939766; -.
DR KEGG; bsu:BSU10110; -.
DR PATRIC; fig|224308.179.peg.1087; -.
DR eggNOG; COG0744; Bacteria.
DR InParanoid; P38050; -.
DR OMA; HNGVDWK; -.
DR PhylomeDB; P38050; -.
DR BioCyc; BSUB:BSU10110-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase 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; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..714
FT /note="Penicillin-binding protein 1F"
FT /id="PRO_0000083180"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..714
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 49..217
FT /note="Transglycosylase"
FT REGION 297..592
FT /note="Transpeptidase"
FT ACT_SITE 87
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 359
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT CONFLICT 120
FT /note="S -> T (in Ref. 1; CAA74517 and 4; AAA71942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 79265 MW; C89C318FA2D81D0E CRC64;
MFKIKKKKLF IPIIILVLTA FLALIGYISI IFLGHYVIDE KKLILHASSK IVDQNGDEVA
SLYTENREPV SINEIPKQVR EAFIAVEDKR FYEHHGIDAK SVGRAVYRDI LAGGKVEGGS
TITQQLAKNI FLTHDKTFLR KTKEVIIAIN LERDYSKDKL LEMYLNQLYF GHGVYGIQAA
SHYYFNKEVK DLTVSEGAVL AAIPKAPSTY SPILHPDKNK ERRDTILGMM NDQGYISAKE
AVTAQGRTLG LHVKKQSETP WFDSYIDLVI KEAEDKYSIS GEQLLQGGYT IKVPLDSKLQ
KTAYQVMKEG SYYPGTDQNA EGSAVFINNK TGGVEAAIGG RDYTSKGYNR VTAVRQPGST
FKPLAVYGPA MQEKKFKPYS LLKDELQSYG DYTPKNYDSR YEGEVTMSDA ITYSKNAPAV
WTLNEIGVET GKSYLKANGI DIPDEGLALA LGGLEKGVSP LQLAGAFHTF AANGTYTEPF
FISSIIDEDG ETIADHKEEG KRVFSKQTSW NMTRMLQQVV KKGTATSGTY HGDLAGKTGS
TSYTGVSGAT KDAWFAGYTP KITGAVWMGY DKTDQNHYLK AGSSYPTRLF KDILTQAGET
GHVFTKPKNV KELESPIELK PVKTLTADYT FKAAGLFTIE LKWDAQEDDR AVYRIYVNKD
GEETLLDSVE GKGSYEIPYA NLFSGASYKI VPYNTQTKRE GEGTDYVQPK LFSS
