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Database: UniProt
Entry: A0A318H1B6_9BURK
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ID   A0A318H1B6_9BURK        Unreviewed;       614 AA.
AC   A0A318H1B6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=C7444_10532 {ECO:0000313|EMBL:PXW96935.1};
OS   Sphaerotilus hippei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=744406 {ECO:0000313|EMBL:PXW96935.1, ECO:0000313|Proteomes:UP000247811};
RN   [1] {ECO:0000313|EMBL:PXW96935.1, ECO:0000313|Proteomes:UP000247811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 566 {ECO:0000313|EMBL:PXW96935.1,
RC   ECO:0000313|Proteomes:UP000247811};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXW96935.1}.
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DR   EMBL; QJJS01000005; PXW96935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318H1B6; -.
DR   OrthoDB; 9789078at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000247811; Unassembled WGS sequence.
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|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   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:UP000247811};
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        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          99..244
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          286..581
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          13..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   614 AA;  67133 MW;  B14210924F2D8156 CRC64;
     MIRDWLERLR GAPRNRSNSR GRGSRATAAR SAAPPPTVQY ASSPLLAAKT PMWRSRLVVV
     GVGIGFTILI GRAVYIQVID QDFYLKQGES RYVKTFTLAG SRGRIVDRNG QILAASVPSP
     SIWAIPRDYK ATAEQHRQLA QLLGMKASDL KTRLTENGNF VWLRRQVDEN TASQIKALGV
     KGIHQQREYR REYPEGEASA HVVGFTNVEE RGQEGMELAF QKELQGRNGS RSVVRDRLGR
     IVEDIGDSVD PQDGRDVELS IDSKVQFFAY QRLREAVSDH AAKAASVVVL DAQSGEVLAM
     ANYPSYLPGE RRSLSGGQLR NRAVTDTFEP GSTMKPFTVA LAMQTGRVRP ETVIQTAPGR
     IQVSGSTITD SHPHGPLTVE QVIQKSSNVG TVKMAMQMQP REMWEMFTSV GLGQKPPLPF
     PGMASGRLRP FKSWRPVEQA TMSYGYGLSV SLLQLARAYT VFARDGQLIP VSMLKNDRVA
     NGVQIVTPEV ARDVRKMLHM ATIAGGTAPR AQTIGYTVAG KTGTAHKQEG KGYADRKYRS
     VFVGLAPASA PRIIVAVMVD EPTVGGYFGG EVAAPVFSKV VQQSLRVMGV PPDMDVSPQM
     VARAQAAPAE RESF
//
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