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Database: UniProt/TrEMBL
Entry: C9XVP1_CROTZ
LinkDB: C9XVP1_CROTZ
Original site: C9XVP1_CROTZ 
ID   C9XVP1_CROTZ            Unreviewed;       588 AA.
AC   C9XVP1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   31-JAN-2018, entry version 46.
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:CBA28017.1};
GN   OrderedLocusNames=Ctu_07170 {ECO:0000313|EMBL:CBA28017.1};
OS   Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA28017.1, ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RX   PubMed=21037008; DOI=10.1128/JB.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-
RT   borne pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
CC       at the division septum. {ECO:0000256|HAMAP-Rule:MF_02080}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
CC       D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
CC       N-acyl substituents of D-alanine. {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; FN543093; CBA28017.1; -; Genomic_DNA.
DR   RefSeq; WP_007767909.1; NC_013282.2.
DR   ProteinModelPortal; C9XVP1; -.
DR   EnsemblBacteria; CBA28017; CBA28017; CTU_07170.
DR   KEGG; ctu:CTU_07170; -.
DR   PATRIC; fig|693216.3.peg.680; -.
DR   HOGENOM; HOG000049554; -.
DR   KO; K03587; -.
DR   OMA; NVGMIKI; -.
DR   OrthoDB; POG091H01T5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002069; Chromosome.
DR   GO; GO:0005887; C:integral component of 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:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 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   Complete proteome {ECO:0000313|Proteomes:UP000002069};
KW   Glycosyltransferase {ECO:0000313|EMBL:CBA28017.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Membrane {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:CBA28017.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02080}.
FT   DOMAIN       70    220       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      260    554       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    307    307       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02080}.
SQ   SEQUENCE   588 AA;  64021 MW;  33C984DA1CE3589C CRC64;
     MKAAAKTLKP KRQEEQANFI SWRFALLCGC ILLALAFLLA RVAWLQIIDP DMLVRQGDMR
     SLRVQEVSTA RGMITDRSGR PLAVSVPVKA IWADPKELHD AGGITLDNRW KALSDALKIP
     LDQLAARVNA NPKGRFIYLA RQVNPDIGDY IKKLKLPGIH LREESRRYYP SGAVTAHLIG
     FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL
     QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNITGTP KDVMRNRTIT
     DVFEPGSTVK PMVVMTALQR GVVQENTVLN TVPYRINGHE IKDVARYSEL TLTGVLQKSS
     NVGVSKLALA MPSSALVDTY SRFGLGKSTN LGLVGERSGL YPQKQRWSDI ERATFSFGYG
     LMVTPLQLAR VYATIGSYGV YRPLSITKVD PPVPGERIFP ESIVRTVVHM MESVALPGGG
     GVKAAIKGYR IAIKTGTAKK VGPDGRYINK YIAYTAGVAP ASNPRFALVV VINDPQAGKY
     YGGAVSAPVF GAIMGGVLRT MNIEPDALTT GEKSEFVINR EEGTGGRS
//
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