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Entry: A0A024EFM5_9PSED
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ID   A0A024EFM5_9PSED        Unreviewed;       580 AA.
AC   A0A024EFM5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=OU5_4528 {ECO:0000313|EMBL:AHZ71607.1};
OS   Pseudomonas mandelii JR-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1147786 {ECO:0000313|EMBL:AHZ71607.1, ECO:0000313|Proteomes:UP000026913};
RN   [1] {ECO:0000313|EMBL:AHZ71607.1, ECO:0000313|Proteomes:UP000026913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR-1 {ECO:0000313|EMBL:AHZ71607.1,
RC   ECO:0000313|Proteomes:UP000026913};
RX   PubMed=22628497; DOI=10.1128/JB.00517-12;
RA   Jang S.H., Kim J., Kim J., Hong S., Lee C.;
RT   "Genome sequence of cold-adapted Pseudomonas mandelii strain JR-1.";
RL   J. Bacteriol. 194:3263-3263(2012).
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; CP005960; AHZ71607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024EFM5; -.
DR   KEGG; pman:OU5_4528; -.
DR   HOGENOM; CLU_009289_6_2_6; -.
DR   OrthoDB; 9789078at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000026913; 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; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          55..204
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          245..545
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        292
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   580 AA;  63020 MW;  0109B4652F0181EC CRC64;
     MMKLEGALFP WRFRLVLGLL GIMVAAICWR IIDLQVVDRA FLKGQGDARS VRHIPIPAHR
     GLITDRNGEP LAVSTPVTTL WANAKEMQLA KEKWPALAAA LGQDPKALAE RLEAQANKEF
     IYLVRGLTPE QGQSVLDLKV PGVYGIEEFR RFYPAGEVTA HMVGFTDIDD HGREGVELAY
     DEWLAGVPGK RQVIKDRRGR LIKDVQVTKN AKAGKPLALS IDLRLQYLAN RELRNAIIEN
     GAKAGSLVIM DVKTGEILAM VNQPTYNPNN RRNLQPAMMR NRAMIDVFEP GSTMKAISMS
     AAIETGRWKP SDTVEVYPGT LQIGKYTIKD VSKSEGPVLD LTGILINSSN VGMSKVAFDI
     GGETIFRLAQ KVGLGQDTGL GFPGERVGNL PNYREWRKAE TATLSYGYGI SVTAIQLVHA
     FSALANNGRL APLTLIKTDK PAQTTQVLPE AVAKTMQTML TQVIEAPRGV FRAQVPAYHV
     GGKSGTARKT SVGTKGYAEN SYRSLFAGFG PMSDPRYAIV VVIDEPTKAG YYGGLVSAPV
     FSKVMSGTLR LMNITPDNLP PTQTANATPV VPLKANGGRG
//
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