ID   FTSI_ECOLI              Reviewed;         588 AA.
AC   P0AD68; P04286;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000305};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331};
DE   AltName: Full=Essential cell division protein FtsI {ECO:0000305};
DE   AltName: Full=Murein transpeptidase {ECO:0000303|PubMed:6450748};
DE   AltName: Full=Penicillin-binding protein 3 {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000303|PubMed:1103132, ECO:0000303|PubMed:7030331};
DE            Short=PBP-3 {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000303|PubMed:7030331};
DE   AltName: Full=Peptidoglycan synthase FtsI {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ftsI {ECO:0000255|HAMAP-Rule:MF_02080,
GN   ECO:0000303|PubMed:7030331}; Synonyms=pbpB;
GN   OrderedLocusNames=b0084, JW0082;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6350821; DOI=10.1007/bf00330881;
RA   Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y.;
RT   "On the process of cellular division in Escherichia coli: nucleotide
RT   sequence of the gene for penicillin-binding protein 3.";
RL   Mol. Gen. Genet. 191:1-9(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   0-2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RC   STRAIN=JE1011;
RX   PubMed=1447153; DOI=10.1128/jb.174.23.7841-7843.1992;
RA   Ueki M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT   "Escherichia coli mraR gene involved in cell growth and division.";
RL   J. Bacteriol. 174:7841-7843(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RX   PubMed=1332942;
RA   Guzman L.-M., Barondess J.J., Beckwith J.;
RT   "FtsL, an essential cytoplasmic membrane protein involved in cell division
RT   in Escherichia coli.";
RL   J. Bacteriol. 174:7716-7728(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-588.
RX   PubMed=2198024; DOI=10.1042/bj2690277;
RA   Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J.;
RT   "Revised interpretation of the sequence containing the murE gene encoding
RT   the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli.";
RL   Biochem. J. 269:277-278(1990).
RN   [8]
RP   FUNCTION IN CELL DIVISION.
RC   STRAIN=K12;
RX   PubMed=1103132; DOI=10.1073/pnas.72.8.2999;
RA   Spratt B.G.;
RT   "Distinct penicillin binding proteins involved in the division, elongation,
RT   and shape of Escherichia coli K12.";
RL   Proc. Natl. Acad. Sci. U.S.A. 72:2999-3003(1975).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=7030331; DOI=10.1016/0006-291x(81)91835-0;
RA   Ishino F., Matsuhashi M.;
RT   "Peptidoglycan synthetic enzyme activities of highly purified penicillin-
RT   binding protein 3 in Escherichia coli: a septum-forming reaction
RT   sequence.";
RL   Biochem. Biophys. Res. Commun. 101:905-911(1981).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RX   PubMed=6450748; DOI=10.1128/jb.145.1.333-340.1981;
RA   Botta G.A., Park J.T.;
RT   "Evidence for involvement of penicillin-binding protein 3 in murein
RT   synthesis during septation but not during cell elongation.";
RL   J. Bacteriol. 145:333-340(1981).
RN   [11]
RP   ACTIVITY REGULATION, AND ACTIVE SITE.
RX   PubMed=3900044; DOI=10.1128/jb.164.1.456-460.1985;
RA   Nicholas R.A., Strominger J.L., Suzuki H., Hirota Y.;
RT   "Identification of the active site in penicillin-binding protein 3 of
RT   Escherichia coli.";
RL   J. Bacteriol. 164:456-460(1985).
RN   [12]
RP   MUTAGENESIS OF SER-307.
RX   PubMed=3911028; DOI=10.1007/bf00331346;
RA   Houba-Herin N., Hara H., Inouye M., Hirota Y.;
RT   "Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia
RT   coli: identification of its active site.";
RL   Mol. Gen. Genet. 201:499-504(1985).
RN   [13]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3531167; DOI=10.1128/jb.168.1.199-206.1986;
RA   Pisabarro A.G., Prats R., Vaquez D., Rodriguez-Tebar A.;
RT   "Activity of penicillin-binding protein 3 from Escherichia coli.";
RL   J. Bacteriol. 168:199-206(1986).
RN   [14]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=2681146; DOI=10.1128/jb.171.11.5890-5893.1989;
RA   Nagasawa H., Sakagami Y., Suzuki A., Suzuki H., Hara H., Hirota Y.;
RT   "Determination of the cleavage site involved in C-terminal processing of
RT   penicillin-binding protein 3 of Escherichia coli.";
RL   J. Bacteriol. 171:5890-5893(1989).
RN   [15]
RP   MUTAGENESIS OF ASN-361.
RX   PubMed=3049550; DOI=10.1128/jb.170.10.4828-4837.1988;
RA   Taschner P.E.M., Ypenburg N., Spratt B.G., Woldringh C.L.;
RT   "An amino acid substitution in penicillin-binding protein 3 creates pointed
RT   polar caps in Escherichia coli.";
RL   J. Bacteriol. 170:4828-4837(1988).
RN   [16]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=2677607; DOI=10.1111/j.1365-2958.1989.tb00278.x;
RA   Bowler L.D., Spratt B.G.;
RT   "Membrane topology of penicillin-binding protein 3 of Escherichia coli.";
RL   Mol. Microbiol. 3:1277-1286(1989).
RN   [17]
RP   FUNCTION IN RECRUITMENT OF FTSN.
RC   STRAIN=K12;
RX   PubMed=9282742; DOI=10.1046/j.1365-2958.1997.4641833.x;
RA   Addinall S.G., Cao C., Lutkenhaus J.;
RT   "FtsN, a late recruit to the septum in Escherichia coli.";
RL   Mol. Microbiol. 25:303-309(1997).
RN   [18]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9379897; DOI=10.1046/j.1365-2958.1997.5041869.x;
RA   Weiss D.S., Pogliano K., Carson M., Guzman L.M., Fraipont C.,
RA   Nguyen-Disteche M., Losick R., Beckwith J.;
RT   "Localization of the Escherichia coli cell division protein Ftsl (PBP3) to
RT   the division site and cell pole.";
RL   Mol. Microbiol. 25:671-681(1997).
RN   [19]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=9614966; DOI=10.1007/s000180050157;
RA   Nguyen-Disteche M., Fraipont C., Buddelmeijer N., Nanninga N.;
RT   "The structure and function of Escherichia coli penicillin-binding protein
RT   3.";
RL   Cell. Mol. Life Sci. 54:309-316(1998).
RN   [20]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=9603865; DOI=10.1128/jb.180.11.2810-2816.1998;
RA   Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.;
RT   "FtsI and FtsW are localized to the septum in Escherichia coli.";
RL   J. Bacteriol. 180:2810-2816(1998).
RN   [21]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9882665; DOI=10.1128/jb.181.2.508-520.1999;
RA   Weiss D.S., Chen J.C., Ghigo J.M., Boyd D., Beckwith J.;
RT   "Localization of FtsI (PBP3) to the septal ring requires its membrane
RT   anchor, the Z ring, FtsA, FtsQ, and FtsL.";
RL   J. Bacteriol. 181:508-520(1999).
RN   [22]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=11703663; DOI=10.1046/j.1365-2958.2001.02640.x;
RA   Chen J.C., Beckwith J.;
RT   "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with
RT   FtsZ during Escherichia coli cell division.";
RL   Mol. Microbiol. 42:395-413(2001).
RN   [23]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=11807049; DOI=10.1128/jb.184.4.904-912.2002;
RA   Mercer K.L., Weiss D.S.;
RT   "The Escherichia coli cell division protein FtsW is required to recruit its
RT   cognate transpeptidase, FtsI (PBP3), to the division site.";
RL   J. Bacteriol. 184:904-912(2002).
RN   [24]
RP   DOMAIN, AND MUTAGENESIS OF ARG-23; LEU-39; GLN-46; GLY-57; SER-61; LEU-62
RP   AND ARG-210.
RX   PubMed=14702319; DOI=10.1128/jb.186.2.490-502.2004;
RA   Wissel M.C., Weiss D.S.;
RT   "Genetic analysis of the cell division protein FtsI (PBP3): amino acid
RT   substitutions that impair septal localization of FtsI and recruitment of
RT   FtsN.";
RL   J. Bacteriol. 186:490-502(2004).
RN   [25]
RP   SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=15601716; DOI=10.1128/jb.187.1.320-328.2005;
RA   Wissel M.C., Wendt J.L., Mitchell C.J., Weiss D.S.;
RT   "The transmembrane helix of the Escherichia coli division protein FtsI
RT   localizes to the septal ring.";
RL   J. Bacteriol. 187:320-328(2005).
RN   [26]
RP   INTERACTION WITH FTSQ.
RC   STRAIN=K12;
RX   PubMed=17185541; DOI=10.1099/mic.0.2006/000265-0;
RA   D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.;
RT   "Three functional subdomains of the Escherichia coli FtsQ protein are
RT   involved in its interaction with the other division proteins.";
RL   Microbiology 153:124-138(2007).
RN   [27]
RP   SUBUNIT, INTERACTION WITH FTSW, AND DOMAIN.
RX   PubMed=20847002; DOI=10.1099/mic.0.040071-0;
RA   Fraipont C., Alexeeva S., Wolf B., van der Ploeg R., Schloesser M.,
RA   den Blaauwen T., Nguyen-Disteche M.;
RT   "The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a
RT   subcomplex in Escherichia coli.";
RL   Microbiology 157:251-259(2011).
CC   -!- FUNCTION: Essential cell division protein that catalyzes cross-linking
CC       of the peptidoglycan cell wall at the division septum (PubMed:1103132,
CC       PubMed:6450748, PubMed:9614966, PubMed:3531167, PubMed:7030331).
CC       Required for localization of FtsN (PubMed:9282742).
CC       {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3531167,
CC       ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331,
CC       ECO:0000269|PubMed:9282742, ECO:0000269|PubMed:9614966}.
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:0000255|HAMAP-
CC         Rule:MF_02080, ECO:0000269|PubMed:3531167,
CC         ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331};
CC   -!- ACTIVITY REGULATION: Inhibited by beta-lactam antibiotics such as
CC       penicillin, moenomycin, macarbomycin, furazlocillin and piperacillin.
CC       Antibiotics inhibit the activity by binding to the catalytic serine.
CC       {ECO:0000269|PubMed:3900044, ECO:0000269|PubMed:6450748,
CC       ECO:0000269|PubMed:7030331}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:6450748}.
CC   -!- SUBUNIT: Homodimer (PubMed:20847002). Forms a complex with FtsW
CC       (PubMed:20847002). Interacts with FtsQ (PubMed:17185541).
CC       {ECO:0000269|PubMed:17185541, ECO:0000269|PubMed:20847002}.
CC   -!- INTERACTION:
CC       P0AD68; P0AEN4: ftsL; NbExp=4; IntAct=EBI-548564, EBI-1119082;
CC       P0AD68; P29131: ftsN; NbExp=3; IntAct=EBI-548564, EBI-1134233;
CC       P0AD68; P06136: ftsQ; NbExp=5; IntAct=EBI-548564, EBI-1130157;
CC       P0AD68; P0ABG4: ftsW; NbExp=7; IntAct=EBI-548564, EBI-1214767;
CC       P0AD68; P02919: mrcB; NbExp=3; IntAct=EBI-548564, EBI-909769;
CC       P0AD68; P46022: mtgA; NbExp=3; IntAct=EBI-548564, EBI-558469;
CC       P0AD68; P58034: ymgF; NbExp=3; IntAct=EBI-548564, EBI-1214577;
CC       P0AD68; Q8DQM0: divIB; Xeno; NbExp=3; IntAct=EBI-548564, EBI-6446264;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02080,
CC       ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Periplasmic
CC       side {ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}. Note=The
CC       bulk of the molecule, except for the N-terminal membrane anchor region,
CC       protrudes into the periplasmic space (PubMed:2677607, PubMed:9614966).
CC       Localizes to the division septum during the later stages of cell growth
CC       and throughout septation (PubMed:9379897, PubMed:9603865,
CC       PubMed:9882665, PubMed:15601716). Localization is dependent on FtsZ,
CC       FtsA, FtsK, FtsQ, FtsL and FtsW, but not on FtsN (PubMed:9603865,
CC       PubMed:9882665, PubMed:11703663, PubMed:11807049).
CC       {ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11807049,
CC       ECO:0000269|PubMed:15601716, ECO:0000269|PubMed:2677607,
CC       ECO:0000269|PubMed:9379897, ECO:0000269|PubMed:9603865,
CC       ECO:0000269|PubMed:9614966, ECO:0000269|PubMed:9882665}.
CC   -!- DOMAIN: Contains an N-terminal membrane anchor-containing module, a
CC       central non-catalytic domain and a C-terminal penicillin-binding (PB)
CC       catalytic domain. The transmembrane region is essential for
CC       localization to the septal ring, interaction with FtsW and cell
CC       septation. {ECO:0000269|PubMed:14702319, ECO:0000269|PubMed:15601716,
CC       ECO:0000269|PubMed:20847002, ECO:0000269|PubMed:9614966}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a bifunctional enzyme with
CC       transglycosylase and transpeptidase activities.
CC       {ECO:0000305|PubMed:7030331}.
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DR   EMBL; K00137; AAA24300.1; -; Genomic_DNA.
DR   EMBL; X55034; CAA38861.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73195.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96652.1; -; Genomic_DNA.
DR   EMBL; S49802; AAB24312.1; -; Genomic_DNA.
DR   EMBL; S49875; AAB24310.1; -; Genomic_DNA.
DR   EMBL; X55814; CAA39333.1; -; Genomic_DNA.
DR   PIR; A93123; ZPECP3.
DR   RefSeq; NP_414626.1; NC_000913.3.
DR   RefSeq; WP_000642196.1; NZ_LN832404.1.
DR   PDB; 6HZQ; X-ray; 1.95 A; A=234-588.
DR   PDB; 6I1I; X-ray; 1.75 A; A=234-279, A=295-588.
DR   PDB; 7ONW; X-ray; 2.70 A; A=49-588.
DR   PDBsum; 6HZQ; -.
DR   PDBsum; 6I1I; -.
DR   PDBsum; 7ONW; -.
DR   AlphaFoldDB; P0AD68; -.
DR   SMR; P0AD68; -.
DR   BioGRID; 4261637; 166.
DR   BioGRID; 849200; 2.
DR   ComplexPortal; CPX-1936; Divisome complex.
DR   DIP; DIP-47950N; -.
DR   IntAct; P0AD68; 18.
DR   MINT; P0AD68; -.
DR   STRING; 511145.b0084; -.
DR   ChEMBL; CHEMBL2354204; -.
DR   DrugBank; DB01602; Bacampicillin.
DR   DrugBank; DB00578; Carbenicillin.
DR   DrugBank; DB09319; Carindacillin.
DR   DrugBank; DB01327; Cefazolin.
DR   DrugBank; DB01413; Cefepime.
DR   DrugBank; DB00267; Cefmenoxime.
DR   DrugBank; DB00274; Cefmetazole.
DR   DrugBank; DB01328; Cefonicid.
DR   DrugBank; DB01329; Cefoperazone.
DR   DrugBank; DB01331; Cefoxitin.
DR   DrugBank; DB00430; Cefpiramide.
DR   DrugBank; DB01416; Cefpodoxime.
DR   DrugBank; DB00438; Ceftazidime.
DR   DrugBank; DB01415; Ceftibuten.
DR   DrugBank; DB04918; Ceftobiprole.
DR   DrugBank; DB09050; Ceftolozane.
DR   DrugBank; DB01000; Cyclacillin.
DR   DrugBank; DB00303; Ertapenem.
DR   DrugCentral; P0AD68; -.
DR   MEROPS; X52.001; -.
DR   jPOST; P0AD68; -.
DR   PaxDb; 511145-b0084; -.
DR   EnsemblBacteria; AAC73195; AAC73195; b0084.
DR   GeneID; 75202099; -.
DR   GeneID; 944799; -.
DR   KEGG; ecj:JW0082; -.
DR   KEGG; eco:b0084; -.
DR   PATRIC; fig|1411691.4.peg.2196; -.
DR   EchoBASE; EB0337; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_2_6; -.
DR   InParanoid; P0AD68; -.
DR   OMA; SCIVVIH; -.
DR   OrthoDB; 9789078at2; -.
DR   PhylomeDB; P0AD68; -.
DR   BioCyc; EcoCyc:EG10341-MONOMER; -.
DR   BioCyc; MetaCyc:EG10341-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:P0AD68; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR   GO; GO:1990586; C:divisome complex; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0008658; F:penicillin binding; IDA:EcoliWiki.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoliWiki.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IMP:EcoliWiki.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0000917; P:division septum assembly; NAS:ComplexPortal.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; NAS:ComplexPortal.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoliWiki.
DR   Gene3D; 1.10.150.770; -; 1.
DR   Gene3D; 3.30.450.330; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   HAMAP; MF_02080; FtsI_transpept; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR037532; FtsI_transpept.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carboxypeptidase; Cell cycle; Cell division;
KW   Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..577
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI"
FT                   /id="PRO_0000017052"
FT   PROPEP          578..588
FT                   /evidence="ECO:0000269|PubMed:2681146"
FT                   /id="PRO_0000017053"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:2677607"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT   TOPO_DOM        40..577
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:2677607"
FT   ACT_SITE        307
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02080,
FT                   ECO:0000269|PubMed:3900044"
FT   MUTAGEN         23
FT                   /note="R->C,H: Impairs septal localization."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         39
FT                   /note="L->P: Impairs septal localization."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         46
FT                   /note="Q->H: Impairs septal localization."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         57
FT                   /note="G->D: Impairs recruitment of FtsN to the septal
FT                   ring."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         61
FT                   /note="S->F,P: Impairs recruitment of FtsN to the septal
FT                   ring."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         62
FT                   /note="L->P: Impairs recruitment of FtsN to the septal
FT                   ring."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         210
FT                   /note="R->C,H: Impairs recruitment of FtsN to the septal
FT                   ring."
FT                   /evidence="ECO:0000269|PubMed:14702319"
FT   MUTAGEN         307
FT                   /note="S->A,T: Unable to bind penicillin."
FT                   /evidence="ECO:0000269|PubMed:3911028"
FT   MUTAGEN         307
FT                   /note="S->C: Still able to bind penicillin."
FT                   /evidence="ECO:0000269|PubMed:3911028"
FT   MUTAGEN         361
FT                   /note="N->S: In PBPBR1; obtained after selection for
FT                   increased resistance to cephalexin, causes a change in the
FT                   shape of the cell: The polar caps are pointed."
FT                   /evidence="ECO:0000269|PubMed:3049550"
FT   STRAND          81..93
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           95..100
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           110..116
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           145..153
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   STRAND          157..168
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   STRAND          188..190
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           192..195
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           238..254
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          258..266
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   TURN            267..269
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          271..279
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           297..300
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           306..309
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           310..319
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          328..330
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          348..351
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           352..357
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           361..369
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           374..382
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   TURN            383..386
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   TURN            394..397
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           409..416
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   TURN            418..420
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   HELIX           425..436
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          439..441
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          445..447
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           461..471
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           472..475
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           482..484
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          492..501
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          503..505
FT                   /evidence="ECO:0007829|PDB:6HZQ"
FT   STRAND          507..519
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   STRAND          521..523
FT                   /evidence="ECO:0007829|PDB:7ONW"
FT   STRAND          526..534
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           542..545
FT                   /evidence="ECO:0007829|PDB:6I1I"
FT   HELIX           547..560
FT                   /evidence="ECO:0007829|PDB:6I1I"
SQ   SEQUENCE   588 AA;  63877 MW;  C89A403D5980B2CD CRC64;
     MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP DMLVKEGDMR
     SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD AGGISVGDRW KALANALNIP
     LDQLSARINA NPKGRFIYLA RQVNPDMADY IKKLKLPGIH LREESRRYYP SGEVTAHLIG
     FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL
     QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT
     DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL TLTGVLQKSS
     NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL YPQKQRWSDI ERATFSFGYG
     LMVTPLQLAR VYATIGSYGI YRPLSITKVD PPVPGERVFP ESIVRTVVHM MESVALPGGG
     GVKAAIKGYR IAIKTGTAKK VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY
     YGGAVSAPVF GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS
//