UniProt: Q5NGX9

Database: UniProt
Entry: Q5NGX9_FRATT

LinkDB:  Q5NGX9_FRATT 
Original site:  Q5NGX9_FRATT

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   Q5NGX9_FRATT            Unreviewed;       564 AA.
AC   Q5NGX9; A0A0G2RPE4;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   ECO:0000313|EMBL:CAG45330.1};
GN   OrderedLocusNames=FTT_0697 {ECO:0000313|EMBL:CAG45330.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45330.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG45330.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(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   -!- 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; AJ749949; CAG45330.1; -; Genomic_DNA.
DR   RefSeq; WP_003020496.1; NZ_CP010290.1.
DR   RefSeq; YP_169713.1; NC_006570.2.
DR   AlphaFoldDB; Q5NGX9; -.
DR   DNASU; 3191383; -.
DR   EnsemblBacteria; CAG45330; CAG45330; FTT_0697.
DR   KEGG; ftu:FTT_0697; -.
DR   PATRIC; fig|177416.36.peg.116; -.
DR   OrthoDB; 9789078at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001174; Chromosome.
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|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   Glycosyltransferase {ECO:0000313|EMBL:CAG45330.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transferase {ECO:0000313|EMBL:CAG45330.1};
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   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          53..204
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          247..547
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        294
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   564 AA;  62699 MW;  9E3BA58CCCA0D3A2 CRC64;
     MSSYRPKLRH FVVIILLLLS FIVLFIKLIY METIQYPKLK QEGDNRSDRS IDIKAYRGII
     LDRNGNPLAI STPVDTIWVD PFYISADSPE LNKVMNILNL PEKTREKIKS QVKVREGRSG
     FVYIERKVQP YLSQKVKDLD ITGIHVIREF KRYYPMAEVA SHIVGFTNVD GKGQEGLELE
     FNKFLSGQDG YFEYKKDLHG GVASKIEDKY VEPKNGRNLQ ISIDSRLQYI AYKYLKEGVI
     RTNSEAGSVI VEDIHIGEIL AMANYPSYNP NSMADAYPDR RRNRAITDVY ELGSVMKTFA
     AATALTYGDN VTSDEPVIDT HPGFYRIGKN TVRDERDYGD INLRHILMKS SNVGVSKMIL
     GLTEPSILES SLRNFGFGSK TGIKLPGERD GYVPTKDKWG DFQLATLSFG YGMNATDLQL
     IAGVSAIANN GQYIKPTILK RRPGEEIETR PIISEKNSKE MISMMQSVVE DLGGTGSKAQ
     IPLYHVAGKT GTARMLSGGN YGAKYLASFV GIVPATDPKL AIVVTIKDPK GDQYGGGSVA
     APVFADVALN SLQILGVKLD KIEN
//

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