ID Q60FV0_HAEIF Unreviewed; 610 AA.
AC Q60FV0;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 56.
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:BAD52394.1};
GN Synonyms=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
OS Haemophilus influenzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727 {ECO:0000313|EMBL:BAD52394.1};
RN [1] {ECO:0000313|EMBL:BAD52394.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HI00127 {ECO:0000313|EMBL:BAD52394.1};
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).
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}.
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DR EMBL; AB186948; BAD52394.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60FV0; -.
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..22
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; 67232 MW; 9F09F5BB8D0133D7 CRC64;
MVKFNSSRKS GKSKKTIRKL TAPETVKQNK SQKVFEKCFM RGRYMLSTVL ILLGLCALVA
RAAYVQSINA DTLSNEADKR SLRKDEVLSV RGSILDRNGQ LLSVSVPMSA IVADPKTMLK
ENSLADKERI AALAEELGMT ENDLVKKIEK NSKSGYLYLA RQVELSKANY IRRLKIKGII
LETEHRRFYP RVEEAAHVVG YTDIDGNGIE GIEKSFNSLL VGKDGSRTVR KDKRGNIVAH
ISDEKKYDAQ DVTLSIDEKL QSMVYREIKK AVSDNNAESG TAVLVDVRTG EVLAMATAPS
YNPNNRVGVK SELMRNRAIT DTFEPGSTVK PFVVLTALQR GVVKRDEIIN TTSFKLNGKE
IVDVAPRAQQ TLDEILMNSS NRGVSRLALR MPPSALMETY QNAGLSKPTD LGLIGEQVGI
LNANRKRWAD IERATVAYGY GITATPLQIA RAYATLGSFG VYRPLSITKV DPPVIGKRVF
SEKITKDIVG ILEKVAIKNK RTMVEGYRVG VKTGTARKIE NGHYVKKYVA FTAGIAPISD
PRYALVVLIN DPKAGEYYGG AVSAPVFSSI MGYALRANAI PQDAESAENT TTKTTKRIVY
IGDHKNQKVN
//
