ID A0A370N244_9BURK Unreviewed; 621 AA.
AC A0A370N244;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
GN ORFNames=DLM46_27770 {ECO:0000313|EMBL:RDJ99574.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDJ99574.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02080}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDJ99574.1}.
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DR EMBL; QHKS01000022; RDJ99574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370N244; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000254875; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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|HAMAP-Rule:MF_02080};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02080,
KW ECO:0000313|EMBL:RDJ99574.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000254875};
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 TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 75..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..607
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 447..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 306
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 621 AA; 65823 MW; C3EACA9EF9095FD6 CRC64;
MIQKKKSQSH DPYAPVAKNP LLTARLPMWR SKLVVLLVFG AFASLAGRAF WVQVVKQDFY
VDQGQKRYQR TIELDATRGR IVDRNGSMLA VSLATYEIWA TPKLLDEAAF PPLSKLLDLP
LAELRRRLTA DKAFVLLKRQ VDADTADHVG KLGLAGITQM ADSKRFYPEG ESAAHVVGFT
DIEDNGQEGV ELAANEQLLG VPGQREVIRD RLGRVVSETR PLVPPQNGQT IHLTIDRRIQ
QLAYAQLKEA IARHHAEAGS VVVLDARNGE ILALANYPSF DPNDRARLTG RQLRNRAVVD
TFEPGSTIKP VVVALSIDQG KVRPQSVIDT APGRYKIGPA VIHDTSNHGA MTVAEAVQKS
SNIALAKLAL NLPAETIWTK YREYGLGLRP ELTFPGVASG KVRPYKRWRP IEQATMAYGY
GLSTSLLQIA QVYTAYAGDG TMHHVSLLRD PTSGSSGSSG SSGSSGSSGS SGSSGSSGAS
GASGSSDASI ASADRAAAAA DAPSATRKGQ TVTTPATARA IRSMLEMATG PGGTGRAAAV
EGYRIGGKTG TARKQVGASY AKNRYRALFV GMAPMSAPRL IVAVMIDDPA GKAFYGGTVA
GPVFSAVTGG ALQLLGVPPD A
//
