ID   FTSI_BUCAI              Reviewed;         579 AA.
AC   P57317;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=BU222;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB12938.1; -; Genomic_DNA.
DR   RefSeq; NP_240052.1; NC_002528.1.
DR   RefSeq; WP_010896013.1; NC_002528.1.
DR   AlphaFoldDB; P57317; -.
DR   SMR; P57317; -.
DR   STRING; 107806.10038903; -.
DR   PRIDE; P57317; -.
DR   EnsemblBacteria; BAB12938; BAB12938; BAB12938.
DR   KEGG; buc:BU222; -.
DR   PATRIC; fig|107806.10.peg.235; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_2_6; -.
DR   OMA; HGKEEYY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001806; 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; Reference proteome; Septation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..579
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI"
FT                   /id="PRO_0000195458"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT   ACT_SITE        305
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   579 AA;  65205 MW;  E3717820808CAD12 CRC64;
     MYKKEKNRFL KSKQINYINW RFFLLYGFIF LSLFILTLRV IFLQIISSNR LITEGDRRTL
     RTQSLLSTRG AIKDRRGYPL AVTVLVNAIC ADPSVILKTK NIKNHKRWQA LSEILSIPLK
     KMFLRINSHK KSKFIYLARQ INPEISEYIK KLQLPGIFLL EESKRYYPFK EISAQLVGFT
     NIDGIGIEGI EKSFDLLLTG KPGKRKIRQD NKGHVIEKIS LVHKRASNNL NLSIDTKLQT
     IVYNELQEGV KKSQSDSGTA ILINIKSGEV LAMANSPSYN PNNIRHIIQK NVRNKAITDL
     FEPGSTVKPI VIIEALKLGI IQENSIIDTK PFLIQKHQIK DVSYHEKLTI TGILQKSSNV
     GVSKIALSMP TLKLLDSYIK FGLGKPTQLG LIGEKHGFFP PKKRWSNLDK ATLSFGYGLM
     VTPLQLARLY STIASYGIYR PLSIIKTDRP TGGKQIFPPK YVKKVINMME SVSQPGGGGL
     QAAVRGYRVA VKTGTAKKVG IHGRYIKKYT AYTAGIAPAS DPRFSLIIIL DNPQGKKYYG
     GAVSAPVFSN IMKLILKKMN IKPDNLSNQK MILKSNKRN