ID B1YSR8_BURA4 Unreviewed; 615 AA.
AC B1YSR8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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};
DE Flags: Precursor;
GN Name=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
GN OrderedLocusNames=BamMC406_0482 {ECO:0000313|EMBL:ACB62979.1};
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB62979.1, ECO:0000313|Proteomes:UP000001680};
RN [1] {ECO:0000313|Proteomes:UP000001680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:5UY7}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 45-615.
RA Edwards T.E., Abendroth J., Lorimer D.,
RA Seattle Structural Genomics Center for Infectious Disease.;
RT "Crystal structure of a peptidoglycan glycosyltransferase from Burkholderia
RT ambifaria.";
RL Submitted (FEB-2017) to the PDB data bank.
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; CP001025; ACB62979.1; -; Genomic_DNA.
DR RefSeq; WP_012363023.1; NC_010551.1.
DR PDB; 5UY7; X-ray; 1.65 A; A=45-615.
DR PDBsum; 5UY7; -.
DR AlphaFoldDB; B1YSR8; -.
DR SMR; B1YSR8; -.
DR KEGG; bac:BamMC406_0482; -.
DR HOGENOM; CLU_009289_6_2_4; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001680; Chromosome 1.
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; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5UY7};
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 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 Glycosyltransferase {ECO:0000313|EMBL:ACB62979.1};
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 Transferase {ECO:0000313|EMBL:ACB62979.1};
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 70..218
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 578..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..615
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 615 AA; 66477 MW; E98F4F9E2C7DBB3F CRC64;
MKPSQKRQDV KFSSSPVLGV HLPMWRSKLV VFMLFMAFVA LAARAFWIQG PGNAFYQKQG
ESRYQRTLEL PATRGKILDR NGLVLATSLP VRAIWAIPDA VPDDLGADKI NQLGKLLGMT
PKELRVKLSE DKGFVYVKRQ VPIDVADKVA ALDIPGIYQR NEYKRFYPEG EITAHLIGFT
NVEDEGQEGV ELGDQKLLSG TSGVRRVIKD RLGHIVEDVA EQVPPHNGTD VGLSIDSKIQ
YIAYANLKAA VEKFKAKAGA AMVVDVRTGE VLALVNYPTY NPNDRTRLTG EQLRNRILTD
VFEPGSIMKP FTVSLALDLH RVTPNTLVET GNGHFVLDGA PITDDAGFGT LTVGGVIQKS
SNIGATKIAM TMRPEEMWNM YTSIGLGQAP KVGFPGAAAG RLRPWKSWRR IEQATMSYGY
GLSVSLFQLA RAYTAIAHDG EMMPVTIFKT DPNQQITGTQ VFTPTTAREV RTMLETVVAP
GGTSPDAAVP GYRVGGKSGT AYKHEGHGYT RKYRASFVGM APMPNPRIVV AVSVDEPTAG
SHFGGQVSGP VFSAIAGDTM RALNVPPNMP IKQLVVSDDA PGAPAKPGPQ KLAAGSGAKH
MIVSSTTRNS PGVVR
//
