FTSI_BUCBP
ID FTSI_BUCBP Reviewed; 576 AA.
AC Q89AQ0;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=bbp_204;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26936.1; -; Genomic_DNA.
DR RefSeq; WP_011091337.1; NC_004545.1.
DR AlphaFoldDB; Q89AQ0; -.
DR SMR; Q89AQ0; -.
DR STRING; 224915.bbp_204; -.
DR EnsemblBacteria; AAO26936; AAO26936; bbp_204.
DR GeneID; 56470746; -.
DR KEGG; bab:bbp_204; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_6; -.
DR OMA; HGKEEYY; -.
DR OrthoDB; 213680at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000601; 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..576
FT /note="Peptidoglycan D,D-transpeptidase FtsI"
FT /id="PRO_0000195460"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT ACT_SITE 308
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
SQ SEQUENCE 576 AA; 65288 MW; EC627ED2F1204CD7 CRC64;
MKYFFQNKKN IHIKNETFNN RITILLSLII ITIILVLSRI TFLQIIVSKK LIYKSNLRSL
RTQIEFNQRG NITDRLGYPL AINIPVKNIC IDPKLLFSKQ THIYPNLKWK MLSTVLSIPL
SEIFYRIKYS KNNHFIYLAH KVNPEISEYI SQLHIPGIYI LDDFKRFYPF GKLTSQLIGF
TNIDNEGIEG VEKSFNKLLM GKPGKKQIIT DRYGRIIEQH NLVNKIQSHD IILSIDCSFQ
KFIYHILNQA VMSNKAKFGV AILVNIPTGE ILSMVNTPSY DPNNSSELFK NNPLIRNKAI
TDIFELGSTV KPMIIMKALE KKIITPETVI NTSSLVVNKH IIHDVSYHHA LTASDILKKS
SNTGVSRLAL SIPISELIDI YSKFELGKST NLGLIGERNG VLNTNKKHWS DLDKVTLSFG
YGLMATPLQL ARIYTTIGRY GLSKPLSIIV KNDTNLKNDI FSKQVFSKKI IKTVINMLEE
VAKPGGAGFK AAIKGYRIAV KTGTAKKINS KGKYDNKYVS YIVGFAPVSN PTFCLMIMIN
EPKSNKYYGG EIAAPIFKTI MQKILKIKNI KPDAYL
