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Database: UniProt
Entry: Q9F1N6_SHEVI
LinkDB: Q9F1N6_SHEVI
Original site: Q9F1N6_SHEVI 
ID   Q9F1N6_SHEVI            Unreviewed;       580 AA.
AC   Q9F1N6;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 62.
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:BAB19196.1};
OS   Shewanella violacea.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60217 {ECO:0000313|EMBL:BAB19196.1};
RN   [1] {ECO:0000313|EMBL:BAB19196.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ishii A., Nakasone K., Sato T., Sugai M., Wachi M., Nagai K., Kato C.;
RT   "Isolation and characterization of dcw gene cluster for cell division and
RT   cell wall synthesis from a deep-sea piezophilic Shewanella violacea.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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; AB052554; BAB19196.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F1N6; -.
DR   OMA; QDNYSLA; -.
DR   UniPathway; UPA00219; -.
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   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   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        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          64..216
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          258..552
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        304
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   580 AA;  64323 MW;  FECF2C843B48323F CRC64;
     MRKIKQAKRK QKPQLIHWRL YVVVAFVCLL FTSLIGRAAY IQILEPEKLR HESDMRSLRT
     TSREVQRGLI TDRNGEMLAI SVPVKAVYAD PKVVNDKNGF ADMRLWQALA DVLHEPEDKI
     LKRVQDHPKR RFTYLKRQVT PAVADYIKKL KLPGIYLKAE SRRYYPTSEI IAQLIGITNI
     DDVGIEGIEN TYNDWLTGTP SKQKVRKSRD GHVVERLDMV QEGESPNDLV LSIDQRIQQL
     AYREIKRVTE INKATSASIV VIDVNTGEVL AMANTPSYNP NSRDHLQSYR MRNRALTDAY
     EPGSTIKPFA VAAALEAGTI NKNQIFKTSP GRIRIGGKIV RDGRNYGDLS LGEVLVHSSN
     VGMTQIALSM PVQELLGYYQ AMGLGNYSGI NLAGESTGLL HDRRRWSEFE RATLSFGYAL
     TVTPLQIARM YAMLGGKGIL YPSSILKLKK KPEGVQVISP EVAQHVMEML IGVTEPGGTA
     TKAHIEGYPV AGKTGTARKA VAGGYGEDYV AMFAGVAPVH NPRLAIAVVV NEPKGDKYYG
     GDVAGPAFAK VMSGALQMLN VEPITSKEKV RLVSHVKRTE
//
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