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Database: UniProt
Entry: A0A2D2MAV2_9PSED
LinkDB: A0A2D2MAV2_9PSED
Original site: A0A2D2MAV2_9PSED 
ID   A0A2D2MAV2_9PSED        Unreviewed;       404 AA.
AC   A0A2D2MAV2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00913};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
GN   Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913,
GN   ECO:0000313|EMBL:ATR84657.1};
GN   ORFNames=CS390_20020 {ECO:0000313|EMBL:ATR84657.1};
OS   Pseudomonas sp. HLS-6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2049589 {ECO:0000313|EMBL:ATR84657.1, ECO:0000313|Proteomes:UP000230810};
RN   [1] {ECO:0000313|EMBL:ATR84657.1, ECO:0000313|Proteomes:UP000230810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLS-6 {ECO:0000313|EMBL:ATR84657.1,
RC   ECO:0000313|Proteomes:UP000230810};
RA   Hu Y., Zhang T., Lei D., Yao S., Lin K., Chen X., Cui C.;
RT   "Complete genome of Pseudomonas sp. HSL-6, a multiple-antibiotic-resistant
RT   bacteria isolated from drinking water source in East China.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988, ECO:0000256|HAMAP-
CC         Rule:MF_00913};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00913}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=Localizes to the
CC       division septum. {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|ARBA:ARBA00038053, ECO:0000256|HAMAP-Rule:MF_00913}.
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DR   EMBL; CP024478; ATR84657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D2MAV2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000230810; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase 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_00913; PGT_FtsW_proteobact; 1.
DR   InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR   InterPro; IPR013437; FtsW.
DR   InterPro; IPR001182; FtsW/RodA.
DR   NCBIfam; TIGR02614; ftsW; 1.
DR   PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR   PANTHER; PTHR30474:SF2; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR   PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00913};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00913};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Reference proteome {ECO:0000313|Proteomes:UP000230810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00913}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        128..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        156..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        179..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        203..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        319..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        355..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ   SEQUENCE   404 AA;  44048 MW;  6B757A1467196053 CRC64;
     MIFGVIKPYP SPLITGRGID LDFPLLAGCL ALLGLGLVMI TSASSEVAAA QSGTPLYHMF
     RHLVYVLLGL GAGVVTIMVP IATWQRMGFL MLVGAFGLLV LVLVPGIGRE VNGSMRWIGF
     SFFNVQPSEI AKVFVVIYLA GYLVRRQTEV RESWMGFFKP FIVLLPMAGL LLMEPDFGAT
     VVMMGAAAAM LFLGGVGLFR FSLMVVLAVG AVFVLVQAQP YRMARLITFT DPWSDQFGSG
     YQLTQALIAF GRGEWFGVGL GNSVQKQFYL PEAHTDFVFS VLAEELGVVG SLATVALFLF
     VTVRSLYIGL WAEKAKQFFA AYMAFGLAFL WIGQFLINIG VNVGLLPTKG LTLPFLSYGG
     SSLVICCACV GLLLRIEWES RTHLGSEEHE FDESDFAEEP NHGR
//
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