FTSI_BUCAP
ID FTSI_BUCAP Reviewed; 568 AA.
AC O85297;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000255|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 3 {ECO:0000255|HAMAP-Rule:MF_02080};
DE Short=PBP-3 {ECO:0000255|HAMAP-Rule:MF_02080};
GN Name=ftsI {ECO:0000255|HAMAP-Rule:MF_02080}; OrderedLocusNames=BUsg_216;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9688822; DOI=10.1007/s002849900365;
RA Thao M.L., Baumann P.;
RT "Sequence analysis of a DNA fragment from Buchnera aphidicola (Aphid
RT endosymbiont) containing the genes dapD-htrA-ilvI-ilvH-ftsL-ftsI-murE.";
RL Curr. Microbiol. 37:214-216(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000255|HAMAP-Rule:MF_02080}.
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02080}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
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DR EMBL; AF060492; AAC32337.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67776.1; -; Genomic_DNA.
DR RefSeq; WP_011053743.1; NC_004061.1.
DR AlphaFoldDB; O85297; -.
DR SMR; O85297; -.
DR STRING; 198804.BUsg_216; -.
DR EnsemblBacteria; AAM67776; AAM67776; BUsg_216.
DR KEGG; bas:BUsg_216; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_6; -.
DR OMA; HGKEEYY; -.
DR OrthoDB; 213680at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Carboxypeptidase; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Septation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="Peptidoglycan D,D-transpeptidase FtsI"
FT /id="PRO_0000195459"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT ACT_SITE 302
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
SQ SEQUENCE 568 AA; 63939 MW; 533B30828687CEE1 CRC64;
MNLFKEKKIK KIIYINWRFV TLCSIVFLFL VILTLRIIFL QIINSKKLAY EGDRRTLRIQ
SVINRRGIIN DRLGYPLAVA VPVNAVFIDP TMITNKNDIK NNIRWKALSE ILSIPLNKLI
FFINSDKNIK FIYLARQINP EIGDYIKALK LPGVFLIEES KRYYPTGAIA AQLIGINNID
GEGIEGIEKS FNSYLTGTPG KRKIRKDNQG QIIENESLIN KSNSNNLILS IDKKLQTIVY
QKLNNAVNEN QADFGIAILI NIETGEILAM ANSPSYNPNN MQYMINKNLR NKAITDIFEP
GSTVKPIVIM EALKRGIIKK NSIINTKPYF IKKHKITDVA YHEKLNITGI LKKSSNVGVS
KIALSMNTSE LINSYIKFGL GQPTNLGLIG EQKGFLPKKK KLSDLEKATF SFGYGLMITP
LQLARLYTII GSYGIYRPLS IIKIDHPLYE KRIFPKRYVK NVIHMMETVA HPGEGGSQAA
IKGYRVAIKT GTAKKVGIHG YYIKKYIAYT AGIAPASNPK FSLTIIIDNP KGEKYYGGAV
SAPVFSKIMK LVLKEMKIKP DNLKNKLS
