ID A0A4Q0ME32_9SPHI Unreviewed; 390 AA.
AC A0A4Q0ME32;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 ORFNames=EKH83_05795 {ECO:0000313|EMBL:RXF71403.1}, F1649_13385
GN {ECO:0000313|EMBL:KAA8481951.1};
OS Arcticibacter tournemirensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=699437 {ECO:0000313|EMBL:RXF71403.1, ECO:0000313|Proteomes:UP000290848};
RN [1] {ECO:0000313|EMBL:RXF71403.1, ECO:0000313|Proteomes:UP000290848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|EMBL:RXF71403.1,
RC ECO:0000313|Proteomes:UP000290848};
RA He J.;
RT "The Draft Genome Sequence of the Soil Bacterium Pedobacter tournemirensis
RT R1.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8481951.1, ECO:0000313|Proteomes:UP000322918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF5-37.2-LB10 {ECO:0000313|EMBL:KAA8481951.1,
RC ECO:0000313|Proteomes:UP000322918};
RA Cai Y.;
RT "Pararcticibacter amylolyticus gen. nov., sp. nov., isolated from a
RT rottenly hemp rope, and reclassification of Pedobacter tournemirensis as
RT Pararcticibacter tournemirensis comb. nov.";
RL Submitted (SEP-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 -!- 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:RXF71403.1}.
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DR EMBL; VWNE01000020; KAA8481951.1; -; Genomic_DNA.
DR EMBL; RXOC01000003; RXF71403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q0ME32; -.
DR OrthoDB; 9812661at2; -.
DR Proteomes; UP000290848; Unassembled WGS sequence.
DR Proteomes; UP000322918; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; 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; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF2; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:RXF71403.1};
KW Cell division {ECO:0000313|EMBL:RXF71403.1};
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:UP000290848};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 390 AA; 42573 MW; ECB064E768D7D09B CRC64;
MNQILSKTKG DRWIWLIVIL LSVWSLLAVY SSTGTIAYKN DKSAEQYLIK HLVMIVGGLA
LMYFSHKLDY RYYAGISKVL MLLTIPLLLY TLIFGATVND ANRWVTIPVI NQTFQTSDLA
KLALITFLAR TLTKKQEQIK DVKRSFLPIM GSVSVVFILI ALANLSTALM LFGVSILLLI
IGRISIKQIL IVCLAGAVLL TGVIFLGPRR KTYASRIETY LHPEKADPDK AFQSNQAKIA
IATGGVFGKG PGNSTQRNYL PHPYSDFVYA LIIEEYGLIG GFVLVLIYLV FLYRCILIVT
ASPKAFGALL AAGLSFSLTI QAFANMAVAV GLGPVTGVPL PLVSMGGTSI LFTSVAFGII
LSVSRDIEEK KKEKDLKGDK VIIGEIPAMG
//
