ID A0A1X8WQN2_LEPIR Unreviewed; 384 AA.
AC A0A1X8WQN2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GNX_1540 {ECO:0000313|EMBL:OCC29988.1}, Lepto782_10905
GN {ECO:0000313|EMBL:QOI42726.1};
OS Leptospira interrogans serovar Canicola.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=211880 {ECO:0000313|EMBL:OCC29988.1, ECO:0000313|Proteomes:UP000093180};
RN [1] {ECO:0000313|EMBL:OCC29988.1, ECO:0000313|Proteomes:UP000093180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tande {ECO:0000313|EMBL:OCC29988.1,
RC ECO:0000313|Proteomes:UP000093180};
RA Kremer F.S., Jorge S., Oliveira N., Woloski R., Sanchez C., Navarro G.O.,
RA Brod C.S., Campos V.F., Pinto L.S., Dellagostin O.;
RT "Genome sequencing of Leptospira interrogans strain Tande.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOI42726.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=782 {ECO:0000313|EMBL:QOI42726.1};
RA Ramli S.R., Bunk B., Goris M., Bhuju S., Jarek M., Sproer C., Mustakim S.,
RA Strommenger B., Pessler F.;
RT "Comparative Genomics of Leptospira interrogans Reveals Genome Plasticity
RT - A Common Adaptive Strategy for Survival in Various Hosts.";
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}.
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DR EMBL; MABU01000034; OCC29988.1; -; Genomic_DNA.
DR EMBL; CP043884; QOI42726.1; -; Genomic_DNA.
DR RefSeq; WP_000606798.1; NZ_CP043884.1.
DR AlphaFoldDB; A0A1X8WQN2; -.
DR GeneID; 61141761; -.
DR Proteomes; UP000093180; Unassembled WGS sequence.
DR Proteomes; UP000663124; Chromosome 1.
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; IPR018365; Cell_cycle_FtsW-rel_CS.
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.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:QOI42726.1};
KW Cell division {ECO:0000313|EMBL:QOI42726.1};
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:UP000093180};
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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 384 AA; 43958 MW; 798909A1EA555D4F CRC64;
MINFIIRKWR EFWLPGKNSL DVLLIVTIFI LLFTGLCVMY SSSSITAWRE FKDSEYFLKK
QTIWICVGLV FFFFFSLFPY QKLEKLALIG IVLAIGLLIL VFIPGIGKSV STYYGRNFHR
WIAIGPYQLQ PSEVAKVAVL VYLASLFQKL KLEITLDYKK LLIPILLLLT VIVLILVEPA
FGTTLEILFV ILGFIFLFGF PFRNLLIAGI VSLPLIYILI DRVGYRKKRV EVWLDPYRYR
FDEGHQLVTS FRAFLDGGWF GNKLASGYAH RYLTYSHTDF VLATFVEDFG FIGFMTFIFL
VLLLLFRSFY LIQKVQDPFG FYLGAGILIV LGTQFIINMF VVTGIFPITG ISLPFVSYGG
SSILIVLISL GILVNITRKE NLGL
//
