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Database: UniProt/TrEMBL
Entry: C3KCS4_PSEFS
LinkDB: C3KCS4_PSEFS
Original site: C3KCS4_PSEFS 
ID   C3KCS4_PSEFS            Unreviewed;       581 AA.
AC   C3KCS4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   31-JAN-2018, entry version 57.
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   OrderedLocusNames=PFLU_0941 {ECO:0000313|EMBL:CAY47207.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47207.1, ECO:0000313|Proteomes:UP000002332};
RN   [1] {ECO:0000313|EMBL:CAY47207.1, ECO:0000313|Proteomes:UP000002332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY47207.1,
RC   ECO:0000313|Proteomes:UP000002332};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY47207.1; -; Genomic_DNA.
DR   RefSeq; WP_012722290.1; NC_012660.1.
DR   ProteinModelPortal; C3KCS4; -.
DR   STRING; 216595.PFLU0941; -.
DR   EnsemblBacteria; CAY47207; CAY47207; PFLU_0941.
DR   KEGG; pfs:PFLU_0941; -.
DR   PATRIC; fig|216595.4.peg.1177; -.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   KO; K03587; -.
DR   OMA; NVGMIKI; -.
DR   OrthoDB; POG091H01T5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002332; 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   ECO:0000313|EMBL:CAY47207.1};
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:UP000002332};
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:CAY47207.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02080}.
FT   DOMAIN       56    205       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      245    545       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    292    292       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02080}.
SQ   SEQUENCE   581 AA;  63271 MW;  B356D64FB865DD1F CRC64;
     MMKLEGALYP WRFRLMLGLL ALMVGAIAWR IIDLQVVDRD FLIGQGDARS LRHIPIPAHR
     GLITDRNGEP LAVSTPVTTL WANAKELQVA KDRWPQLAAA LGQDPKALAE RLEAQANKEF
     IYLVRGLTPE QGQQVLDLKV PGVYGIEEFR RFYPAGETTA HMVGFTDIDD HGREGVELAY
     DEWLAGVPGK RQVIKDRRGR LIKDVQVTKN AKAGKPLALS IDLRLQYLAN RELRNAIIEN
     GAKAGSLVIM DVKTGEILAM VNQPTYNPNN RRNLQPAMMR NRAMIDVFEP GSTMKAISMS
     AALETGRWKP SDKVEVYPGT LQLGKYTIRD VSRTEGPVLD LTGILINSSN VGMSKVAFDI
     GGETIYHLAQ KIGLGQPTGL DFPGERVGNL PNYRDWKKAE TATLSYGYGL SVTAIQLAHA
     FSVLANNGRM VPLSLIHVDE APKATQVIPE NVAKTMQGML QQVIEAPRGV FRAQVPAYHV
     AGKSGTARKT SVGTKGYAEN SYRSLFAGFG PMSDPRYAIV VVIDEPSKAG YFGGLVSAPV
     FSKVMSGTLR LMNITPDNLP PTQQANAGPP AAAVKANGGR G
//
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