ID A0A158AK68_9BURK Unreviewed; 598 AA.
AC A0A158AK68;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AWB78_01722 {ECO:0000313|EMBL:SAK58192.1};
OS Caballeronia calidae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAK58192.1, ECO:0000313|Proteomes:UP000071859};
RN [1] {ECO:0000313|EMBL:SAK58192.1, ECO:0000313|Proteomes:UP000071859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29321 {ECO:0000313|EMBL:SAK58192.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; FCOX02000006; SAK58192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158AK68; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000071859; 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 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 TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 105..248
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 289..584
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 598 AA; 64775 MW; B97BC0DE22038ED1 CRC64;
MAPISTPPSH ACHKRVPDAS PGTTKLNHKT TMFKKKTRGG SDFQTHHRST VLATQLPAWR
SRLVIIGVTA AFMALAGRAL WVQVIDHKFY IGEGQKRYQR TLALSATRGR IVDRNGAMLA
VSLATYEVWA TPRLFDGDHG NEIARLLDMP PKDLQRRIDG NRAFVLLKRQ VEAETAERIA
TIGRAGITLV PDTKRFYPEG ESAAHVVGFT NNEDHGQEGV ELAADARLTG EAGQREVIRD
RLGRIVSQIG EIDLPQNGET IQLTIDRRIQ QLAHAQLKAA IAKHKARAGS VVVLDAKNGE
VLALANYPSF DPNDRARLTG EQLRNRALTD TFEPGSTIKP LVAALAIDLG KVRPDTRIDT
GPGSFKLGPN VIHDTSNHGV ITVAQAVQMS SNIALTKLAL QLPAQTIWDK YREYGIGRAP
ELTFPGAATG RLRAPERWKP IEQATMAYGY GMSLSLVQIA QIYTAYAGDG RFHAATLIHR
ETRREPLQVT KPATAKAVRE MLEMAIGDHG TGRAAAVEGY RVGGKTGTAR KQIGRSYAAN
KYRASFVGIA PMSDPRVIVA VMIDEPTGGT YYGGTVAGPV FSGIVGATLP LLGVPPDA
//
