FTSW_METCA
ID FTSW_METCA Reviewed; 398 AA.
AC Q604V6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_00913};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell division protein FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
GN Name=ftsW {ECO:0000255|HAMAP-Rule:MF_00913}; OrderedLocusNames=MCA2430;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00913};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00913}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00913}. Note=Localizes to the division septum.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
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DR EMBL; AE017282; AAU91478.1; -; Genomic_DNA.
DR RefSeq; WP_010961655.1; NC_002977.6.
DR AlphaFoldDB; Q604V6; -.
DR SMR; Q604V6; -.
DR STRING; 243233.MCA2430; -.
DR EnsemblBacteria; AAU91478; AAU91478; MCA2430.
DR KEGG; mca:MCA2430; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_1_6; -.
DR OMA; KLWWSNL; -.
DR OrthoDB; 1133883at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR TIGRFAMs; TIGR02614; ftsW; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..398
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000415197"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 42..57
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 79..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 114..121
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 143..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 175..177
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 221..289
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 311..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 340..355
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 377..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 42841 MW; 9E721C05A106152B CRC64;
MSTQAIRGAR GLVLKWGAGR FYLDTVLLSV SLGLMLFGFV MVSSASLHLG EKMASDSFYF
PKHQLVHILL GLAAGWGAAR VRLDTLERHS RSLFWAGIAL LVLVLIPGVG KSVNGSVRWI
NLFGLRVQVS EVFKLVAAIY VAGYISRHLD TVRTSVKGMI FPLSLLAIGA VLLLKEPDFG
ATAVVMATAL GMLFLAGARL WVFVGLLGLV AVAGTVLIYT AEYRLRRVLS FLDPWADPLN
SGFQLTQALI AFGRGEWQGV GLGSSVQKLF YLPEAHTDFL FSVIGEELGL WGATTVILLF
AIVVWRALAI GRLAERSGNL FAAFLAYGIG IWLGLQSFIN MGVNMGMLPT KGLTLPLMSY
GGGSMMVVCA AIGLLFRIRS EAVASFLGNG RKGLWPGV
