ID Q60FT7_HAEIF Unreviewed; 610 AA.
AC Q60FT7;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000256|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 3 {ECO:0000256|HAMAP-Rule:MF_02080};
DE Short=PBP-3 {ECO:0000256|HAMAP-Rule:MF_02080};
GN Name=pbp3 {ECO:0000313|EMBL:BAD52407.1};
GN Synonyms=ftsI {ECO:0000256|HAMAP-Rule:MF_02080,
GN ECO:0000313|EMBL:AFC37203.1};
OS Haemophilus influenzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727 {ECO:0000313|EMBL:BAD52407.1};
RN [1] {ECO:0000313|EMBL:BAD52407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HI00130 {ECO:0000313|EMBL:BAD52397.1}, HI00140
RC {ECO:0000313|EMBL:BAD52407.1}, HI00142 {ECO:0000313|EMBL:BAD52409.1},
RC and HI00144 {ECO:0000313|EMBL:BAD52411.1};
RX PubMed=15980357; DOI=10.1128/AAC.49.7.2834-2839.2005;
RA Osaki Y., Sanbongi Y., Ishikawa M., Kataoka H., Suzuki T., Maeda K.,
RA Ida T.;
RT "Genetic approach to study the relationship between penicillin-binding
RT protein 3 mutations and Haemophilus influenzae beta-lactam resistance by
RT using site-directed mutagenesis and gene recombinants.";
RL Antimicrob. Agents Chemother. 49:2834-2839(2005).
RN [2] {ECO:0000313|EMBL:BAF48349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSC02070 {ECO:0000313|EMBL:BAF48349.1};
RX PubMed=17325223; DOI=10.1128/AAC.01545-06;
RA Takahata S., Ida T., Senju N., Sanbongi Y., Miyata A., Maebashi K.,
RA Hoshiko S.;
RT "Horizontal gene transfer of ftsI, encoding penicillin-binding protein 3,
RT in Haemophilus influenzae.";
RL Antimicrob. Agents Chemother. 51:1589-1595(2007).
RN [3] {ECO:0000313|EMBL:AFC37203.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HCM0028 {ECO:0000313|EMBL:AFC37203.1};
RX PubMed=23308379; DOI=10.1089/mdr.2012.0116;
RA Park C., Kim K.H., Shin N.Y., Byun J.H., Kwon E.Y., Lee J.W., Kwon H.J.,
RA Choi E.Y., Lee D.G., Sohn W.Y., Kang J.H.;
RT "Genetic diversity of the ftsI gene in ?-lactamase-nonproducing ampicillin-
RT resistant and ?-lactamase-producing amoxicillin-/clavulanic acid-resistant
RT nasopharyngeal Haemophilus influenzae strains isolated from children in
RT South Korea.";
RL Microb. Drug Resist. 19:224-230(2013).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02080};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN944462; AFC37203.1; -; Genomic_DNA.
DR EMBL; AB186951; BAD52397.1; -; Genomic_DNA.
DR EMBL; AB186961; BAD52407.1; -; Genomic_DNA.
DR EMBL; AB186963; BAD52409.1; -; Genomic_DNA.
DR EMBL; AB186965; BAD52411.1; -; Genomic_DNA.
DR EMBL; AB267863; BAF48349.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60FT7; -.
DR DrugBank; DB00535; Cefdinir.
DR UniPathway; UPA00219; -.
DR GO; GO:0005886; C: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; 1.10.150.770; -; 1.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW Rule:MF_02080}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02080};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02080};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02080};
KW Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02080};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02080}.
FT DOMAIN 90..240
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 280..571
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 610 AA; 67296 MW; A9EDF8623D598081 CRC64;
MVKFNSSRKS GKSKKTIRKL TAPETVKQNK PQKVFEKCFM RGRYMLSTVL ILLGLCALVA
RAAYVQSINA DTLSNEADKR SLRKDEVLSV RGSILDRNGQ LLSVSVPMSA IVADPKTMLK
ENSLADKERI AALAEELGMT ENDLVKKIEK NSKSGYLYLA RQVELSKANY IRRLKIKGII
LETEHRRFYP RVEEAAHVVG YTDIDGNGIE GIEKSFNSLL VGKDGSRTVR KDKRGNIVEH
ISDEKKYDAQ DVTLSIDEKL QSMVYREIKK AVSENNAESG TAVLVDVRTG EVLAMATAPS
YNPNNRVGVK SELMRNRAIT DTFEPGSTVK PFVVLTALQR GVVKRDEIIN TTSFKLNGKE
IVDVAPRAQQ TLDEILINSS NRGVTRLAFR MPPSALMETY QNAGLSKPTD LGLIGEQVGI
LNANRKRWAD IERATVAYGY GITATPLQIA RAYATLGSFG VYRPLSITKV DPPVIGKRVF
SEKITKDIVG ILEKVAIKNK RAMVEGYRVG VKTGTARKIE NGHYVKKYVA FTAGIAPISD
PRYALVILIN DPKAGEYYGG ALSAPVFSSI MGYALRANAI PQDAEAAENT TTKSAKRIVY
IGEHKNQKVN
//