ID A0A368L281_9BURK Unreviewed; 626 AA.
AC A0A368L281;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=DU000_08960 {ECO:0000313|EMBL:RCS57561.1};
OS Parvibium lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Parvibium.
OX NCBI_TaxID=1888893 {ECO:0000313|EMBL:RCS57561.1, ECO:0000313|Proteomes:UP000252357};
RN [1] {ECO:0000313|EMBL:RCS57561.1, ECO:0000313|Proteomes:UP000252357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMB9 {ECO:0000313|EMBL:RCS57561.1,
RC ECO:0000313|Proteomes:UP000252357};
RX PubMed=29498621; DOI=10.1099/ijsem.0.002667;
RA Chen W.M., Xie P.B., Hsu M.Y., Sheu S.Y.;
RT "Parvibium lacunae gen. nov., sp. nov., a new member of the family
RT Alcaligenaceae isolated from a freshwater pond.";
RL Int. J. Syst. Evol. Microbiol. 68:1291-1299(2018).
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:RCS57561.1}.
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DR EMBL; QPGB01000003; RCS57561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368L281; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000252357; 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 Reference proteome {ECO:0000313|Proteomes:UP000252357};
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 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 93..256
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 299..597
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 345
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 626 AA; 68181 MW; 9B319AFEC4EBF6E1 CRC64;
MSELGLQHGG VKVGAKAGAT GTKRGSGANK RGVSFSANPV LNLSLPRWRS RLLLVLIALA
FLALIARAVY LQGFSTDFLQ RQGESRYART LELPATRGKI LDRNGVVLAS SVPAKAIWAI
PDDVMEISKN EKISLAQREQ EWRERLAKLP QLASLLNLPL TELKRKLQAD RSFVYLRRQV
DLDVAEKIAA LKIAGIHERD EYKRYYPEGE TLAHVVGFTN IEDLGQEGVE LSMQQALVGV
NGSRRVIKDR LGRVIEDMGS TQPPRDGRDL TLSIDTRIQY VVYSQLKQAM QQHRAKAAAA
VVLDVQTGEV LALANFPTYN PNQRSHLSGA ELRNRVLTDA FEPGSTLKPF TVALGLEQRL
ITPQKQIQTA PGKLTIGTAT IGDAHPHGWL TVEEIVQKSS NVGTAKIALQ IEREVMWSFL
TELGFGQAPR VGFPGATAGR VRPWKSWRPI EQATMSYGHG ISVSLIQLAR AYSIFARDGD
LVPLSFQKLN AGGQPLVTQR VVSAKTAQSV RKMLEMAAGP GGTAPKAQVI GYSVAGKTGT
AHKLGKQGYE NRYVSSFAGF APVGQPRIII AVMVDEPSAG KHYGGEVAAP IYSAIVENAM
RILQIQPDIP HKTEIVVPAE VLEEGV
//
