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Penicillin-binding protein 1F (PBP-1F) (Penicillin-binding protein F) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPF_BACSU              Reviewed;         714 AA.
P38050;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=Penicillin-binding protein 1F;
Short=PBP-1F;
AltName: Full=Penicillin-binding protein F;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
AltName: Full=DD-transpeptidase;
Name=pbpF; Synonyms=ponA; OrderedLocusNames=BSU10110;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9579061; DOI=10.1099/00221287-144-4-859;
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R.,
Wedler H., Venema G., Bron S.;
"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the
Bacillus subtilis chromosome contains several dysfunctional genes, the
glyB marker, many genes encoding transporter proteins, and the
ubiquitous hit gene.";
Microbiology 144:859-875(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION TO 120.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
STRAIN=168;
PubMed=8335642; DOI=10.1128/jb.175.15.4870-4876.1993;
Popham D.L., Setlow P.;
"Cloning, nucleotide sequence, and regulation of the Bacillus subtilis
pbpF gene, which codes for a putative class A high-molecular-weight
penicillin-binding protein.";
J. Bacteriol. 175:4870-4876(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-714.
PubMed=1459957; DOI=10.1128/jb.174.24.8081-8093.1992;
Hansson M., Hederstedt L.;
"Cloning and characterization of the Bacillus subtilis hemEHY gene
cluster, which encodes protoheme IX biosynthetic enzymes.";
J. Bacteriol. 174:8081-8093(1992).
-!- FUNCTION: Cell wall formation. May be involved in outgrowth of the
germinated spore or it could function in the synthesis of the germ
cell wall.
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000250|UniProtKB:P02918}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000250|UniProtKB:P02918}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
-!- DEVELOPMENTAL STAGE: Expression remains constant during vegetative
growth, decreases during early sporulation, and is induced in the
forespore during late sporulation.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
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EMBL; Y14083; CAA74517.1; -; Genomic_DNA.
EMBL; AL009126; CAB12851.2; -; Genomic_DNA.
EMBL; L10630; AAA71942.1; -; Genomic_DNA.
EMBL; M97208; AAA22516.1; -; Genomic_DNA.
PIR; A40614; A40614.
RefSeq; NP_388892.2; NC_000964.3.
RefSeq; WP_003233213.1; NZ_JNCM01000035.1.
ProteinModelPortal; P38050; -.
SMR; P38050; -.
IntAct; P38050; 1.
STRING; 224308.Bsubs1_010100005621; -.
CAZy; GT51; Glycosyltransferase Family 51.
PaxDb; P38050; -.
EnsemblBacteria; CAB12851; CAB12851; BSU10110.
GeneID; 939766; -.
KEGG; bsu:BSU10110; -.
PATRIC; fig|224308.179.peg.1087; -.
eggNOG; ENOG4105BZ4; Bacteria.
eggNOG; COG0744; LUCA.
HOGENOM; HOG000041137; -.
InParanoid; P38050; -.
KO; K12555; -.
OMA; PAKVYAR; -.
PhylomeDB; P38050; -.
BioCyc; BSUB:BSU10110-MONOMER; -.
UniPathway; UPA00219; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 2.
2: Evidence at transcript level;
Carboxypeptidase; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 714 Penicillin-binding protein 1F.
/FTId=PRO_0000083180.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 34 714 Extracellular. {ECO:0000255}.
REGION 49 217 Transglycosylase.
REGION 297 592 Transpeptidase.
ACT_SITE 87 87 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 359 359 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
CONFLICT 120 120 S -> T (in Ref. 1; CAA74517 and 4;
AAA71942). {ECO:0000305}.
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


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