GenomeNet

Database: UniProt/SWISS-PROT
Entry: FTSI_ECOLI
LinkDB: FTSI_ECOLI
Original site: 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   10-OCT-2018, entry version 116.
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; 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.,
RA   Isono K., 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.,
RA   Mau B., 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
RT   MG1655 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
RT   division 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
RT   encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia
RT   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,
RT   elongation, 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
RT   penicillin-binding protein 3 in Escherichia coli: a septum-forming
RT   reaction sequence.";
RL   Biochem. Biophys. Res. Commun. 101:905-911(1981).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RX   PubMed=6450748;
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;
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
RT   Escherichia 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
RT   of 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
RT   pointed 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
RT   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
RT   (PBP3) to 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
RT   protein 3.";
RL   Cell. Mol. Life Sci. 54:309-316(1998).
RN   [20]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=9603865;
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;
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
RT   with 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
RT   recruit its cognate transpeptidase, FtsI (PBP3), to the division
RT   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;
RP   LEU-62 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
RT   of 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
RT   form a subcomplex in Escherichia coli.";
RL   Microbiology 157:251-259(2011).
CC   -!- FUNCTION: Essential cell division protein that catalyzes cross-
CC       linking of the peptidoglycan cell wall at the division septum
CC       (PubMed:1103132, PubMed:6450748, PubMed:9614966, PubMed:3531167,
CC       PubMed:7030331). Required for localization of FtsN
CC       (PubMed:9282742). {ECO:0000269|PubMed:1103132,
CC       ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748,
CC       ECO:0000269|PubMed:7030331, ECO:0000269|PubMed:9282742,
CC       ECO:0000269|PubMed:9614966}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
CC       D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
CC       N-acyl substituents of D-alanine. {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
CC       piperacillin. Antibiotics inhibit the activity by binding to the
CC       catalytic serine. {ECO:0000269|PubMed:3900044,
CC       ECO:0000269|PubMed:6450748, 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       Q8DQM0:divIB (xeno); NbExp=3; IntAct=EBI-548564, EBI-6446264;
CC       P0AEN4:ftsL; NbExp=4; IntAct=EBI-548564, EBI-1119082;
CC       P29131:ftsN; NbExp=3; IntAct=EBI-548564, EBI-1134233;
CC       P06136:ftsQ; NbExp=5; IntAct=EBI-548564, EBI-1130157;
CC       P0ABG4:ftsW; NbExp=7; IntAct=EBI-548564, EBI-1214767;
CC       P02919:mrcB; NbExp=3; IntAct=EBI-548564, EBI-909769;
CC       P46022:mtgA; NbExp=3; IntAct=EBI-548564, EBI-558469;
CC       P58034:ymgF; NbExp=3; IntAct=EBI-548564, EBI-1214577;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02080, ECO:0000269|PubMed:2677607,
CC       ECO:0000269|PubMed:9614966}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607,
CC       ECO:0000269|PubMed:9614966}; Periplasmic side
CC       {ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}. Note=The
CC       bulk of the molecule, except for the N-terminal membrane anchor
CC       region, protrudes into the periplasmic space (PubMed:2677607,
CC       PubMed:9614966). Localizes to the division septum during the later
CC       stages of cell growth and throughout septation (PubMed:9379897,
CC       PubMed:9603865, PubMed:9882665, PubMed:15601716). Localization is
CC       dependent on FtsZ, FtsA, FtsK, FtsQ, FtsL and FtsW, but not on
CC       FtsN (PubMed:9603865, PubMed:9882665, PubMed:11703663,
CC       PubMed:11807049). {ECO:0000269|PubMed:11703663,
CC       ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:15601716,
CC       ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9379897,
CC       ECO:0000269|PubMed:9603865, ECO:0000269|PubMed:9614966,
CC       ECO:0000269|PubMed:9882665}.
CC   -!- DOMAIN: Contains an N-terminal membrane anchor-containing module,
CC       a central non-catalytic domain and a C-terminal penicillin-binding
CC       (PB) 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,
CC       ECO:0000269|PubMed:15601716, ECO:0000269|PubMed:20847002,
CC       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}.
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   ProteinModelPortal; P0AD68; -.
DR   SMR; P0AD68; -.
DR   BioGrid; 4261637; 166.
DR   DIP; DIP-47950N; -.
DR   IntAct; P0AD68; 18.
DR   MINT; P0AD68; -.
DR   STRING; 316385.ECDH10B_0066; -.
DR   ChEMBL; CHEMBL2354204; -.
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; DB01332; Ceftizoxime.
DR   DrugBank; DB04918; Ceftobiprole.
DR   DrugBank; DB00303; Ertapenem.
DR   PaxDb; P0AD68; -.
DR   PRIDE; P0AD68; -.
DR   EnsemblBacteria; AAC73195; AAC73195; b0084.
DR   EnsemblBacteria; BAB96652; BAB96652; BAB96652.
DR   GeneID; 944799; -.
DR   KEGG; ecj:JW0082; -.
DR   KEGG; eco:b0084; -.
DR   PATRIC; fig|1411691.4.peg.2196; -.
DR   EchoBASE; EB0337; -.
DR   EcoGene; EG10341; ftsI.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   HOGENOM; HOG000049554; -.
DR   InParanoid; P0AD68; -.
DR   KO; K03587; -.
DR   OMA; NVGMIKI; -.
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:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoliWiki.
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; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0042493; P:response to drug; IMP:EcoliWiki.
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   Carboxypeptidase; Cell cycle; Cell division; Cell inner membrane;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Hydrolase; Membrane; Peptidoglycan synthesis;
KW   Protease; Reference proteome; Septation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    577       Peptidoglycan D,D-transpeptidase FtsI.
FT                                /FTId=PRO_0000017052.
FT   PROPEP      578    588       {ECO:0000269|PubMed:2681146}.
FT                                /FTId=PRO_0000017053.
FT   TOPO_DOM      1     18       Cytoplasmic.
FT                                {ECO:0000269|PubMed:2677607}.
FT   TRANSMEM     19     39       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_02080}.
FT   TOPO_DOM     40    577       Periplasmic.
FT                                {ECO:0000269|PubMed:2677607}.
FT   ACT_SITE    307    307       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_02080,
FT                                ECO:0000269|PubMed:3900044}.
FT   MUTAGEN      23     23       R->C,H: Impairs septal localization.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN      39     39       L->P: Impairs septal localization.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN      46     46       Q->H: Impairs septal localization.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN      57     57       G->D: Impairs recruitment of FtsN to the
FT                                septal ring.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN      61     61       S->F,P: Impairs recruitment of FtsN to
FT                                the septal ring.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN      62     62       L->P: Impairs recruitment of FtsN to the
FT                                septal ring.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN     210    210       R->C,H: Impairs recruitment of FtsN to
FT                                the septal ring.
FT                                {ECO:0000269|PubMed:14702319}.
FT   MUTAGEN     307    307       S->A,T: Unable to bind penicillin.
FT                                {ECO:0000269|PubMed:3911028}.
FT   MUTAGEN     307    307       S->C: Still able to bind penicillin.
FT                                {ECO:0000269|PubMed:3911028}.
FT   MUTAGEN     361    361       N->S: In PBPBR1; obtained after selection
FT                                for increased resistance to cephalexin,
FT                                causes a change in the shape of the cell:
FT                                The polar caps are pointed.
FT                                {ECO:0000269|PubMed:3049550}.
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
//
DBGET integrated database retrieval system