FTSI_ECOLI
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 03-AUG-2022, entry version 139.
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, ECO:0000303|PubMed:7030331};
GN Synonyms=pbpB; OrderedLocusNames=b0084, JW0082;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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 0-
RT 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; 7ONW; X-ray; 2.70 A; A=49-588.
DR PDBsum; 6HZQ; -.
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; P0AD68; -.
DR PRIDE; P0AD68; -.
DR EnsemblBacteria; AAC73195; AAC73195; b0084.
DR EnsemblBacteria; BAB96652; BAB96652; BAB96652.
DR GeneID; 66671626; -.
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; HGKEEYY; -.
DR PhylomeDB; P0AD68; -.
DR BioCyc; EcoCyc:EG10341-MON; -.
DR BioCyc; MetaCyc:EG10341-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IC: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; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC: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; 3.40.710.10; -; 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 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 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:6HZQ"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:6HZQ"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:6HZQ"
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:6HZQ"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7ONW"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7ONW"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:6HZQ"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:6HZQ"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:7ONW"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 507..523
FT /evidence="ECO:0007829|PDB:6HZQ"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:6HZQ"
FT TURN 543..546
FT /evidence="ECO:0007829|PDB:6HZQ"
FT HELIX 547..560
FT /evidence="ECO:0007829|PDB:6HZQ"
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
