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Database: UniProt
Entry: A0A4U6Q7R4_9ACTN
LinkDB: A0A4U6Q7R4_9ACTN
Original site: A0A4U6Q7R4_9ACTN 
ID   A0A4U6Q7R4_9ACTN        Unreviewed;       489 AA.
AC   A0A4U6Q7R4;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|ARBA:ARBA00041185};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|ARBA:ARBA00041418};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|ARBA:ARBA00033270};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|ARBA:ARBA00032370};
GN   Name=ftsW {ECO:0000313|EMBL:TKV56088.1};
GN   ORFNames=FDO65_21115 {ECO:0000313|EMBL:TKV56088.1};
OS   Nakamurella flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC   Nakamurella.
OX   NCBI_TaxID=2576308 {ECO:0000313|EMBL:TKV56088.1, ECO:0000313|Proteomes:UP000306985};
RN   [1] {ECO:0000313|EMBL:TKV56088.1, ECO:0000313|Proteomes:UP000306985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5BH11 {ECO:0000313|EMBL:TKV56088.1,
RC   ECO:0000313|Proteomes:UP000306985};
RA   Tuo L.;
RT   "Nakamurella sp. N5BH11, whole genome shotgun sequence.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|ARBA:ARBA00038053}.
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:TKV56088.1}.
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DR   EMBL; SZZH01000008; TKV56088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U6Q7R4; -.
DR   Proteomes; UP000306985; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000306985};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          380..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  51056 MW;  BD598F5639283678 CRC64;
     MASLHLIQAI FALLLGFGLL MVLSSSSVTA FRTGGSSFGV FANQATFALV GLVLFGATQY
     LPVRLMRSLS TAAVMFSILL LVAVLIPGVG KLVNGARSWI AIGGFQFQPS EVAKLALLLW
     MGHVLAARRS TLASPRSLLI PVLPVFILIA GLIMMQPDLG TTTALLIVFM ACLFFAGAPW
     WMFATLAGLA VLGVTALALS ATYRLARVLS FLNPDPTSAS GWQLAQSLYG MGNGGIFGVG
     LGQSRAKWSY LPNADSDFIF AIVGEELGFI GAALLLLLFG LLAYTGLRIA RRNVDPFVKI
     VASAGTVWLV GQAGINICYV VGLLPVTGIP LPMISAGGTS LIITMVVFGL LANFARSEPE
     AAAVLQANGG NRLARFLGVN PKPGAGAKRA AKRTAKAERR AAKSAKRAAA AKPAPARKPA
     SPTRRTPDAV RAEPRSRGAA PRPTTGTQRP GAIPRQPDGR RGAAGARPAR STPSANPRRN
     PSSGGSPQW
//
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