ID A0A6B8VWR4_9CORY Unreviewed; 492 AA.
AC A0A6B8VWR4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=ftsW2 {ECO:0000313|EMBL:QGU01720.1};
GN ORFNames=CKALI_04205 {ECO:0000313|EMBL:QGU01720.1};
OS Corynebacterium kalinowskii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2675216 {ECO:0000313|EMBL:QGU01720.1, ECO:0000313|Proteomes:UP000427071};
RN [1] {ECO:0000313|Proteomes:UP000427071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1959 {ECO:0000313|Proteomes:UP000427071};
RA Schaffert L., Ruwe M., Milse J., Hanuschka K., Ortseifen V., Droste J.,
RA Brandt D., Schlueter L., Kutter Y., Vinke S., Viehoefer P., Jacob L.,
RA Luebke N.-C., Schulte-Berndt E., Hain C., Linder M., Schmidt P.,
RA Wollenschlaeger L., Luttermann T., Thieme E., Hassa J., Haak M.,
RA Wittchen M., Mentz A., Persicke M., Busche T., Ruckert C.;
RT "Complete genome sequence of Corynebacterium kalinowskii 1959, a novel
RT Corynebacterium species isolated from soil of a small paddock in
RT Vilsendorf, Germany.";
RL Submitted (NOV-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}.
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DR EMBL; CP046452; QGU01720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6B8VWR4; -.
DR KEGG; ckw:CKALI_04205; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000427071; Chromosome.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 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:UP000427071};
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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 416..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 53464 MW; 515059749C2D32BF CRC64;
MTAPKATPRE GVWQKITGVI ADLHSRPLTN YTMIMISVSM LTVLGVVMVF SSSMATSVVD
GSSVWSIASR QAFMVVVGLV AMWVAMRIRP ATIRRFAPWF MAVAIVLLIA VLIPGIGTGR
EEVGSQSWIA FGPIRFQPSE FAKVAIAIWG ASFLGVSDEM IKANKRFSIF IVVAAFMTLL
IIAEGDVGMA MTFLLMVAVV LFFAGVDLKV IIGAAGLALL GLVAIMLGSG FRSQRFTVYF
DALFGRFHDT RASSFQSYQG FLSLADGSAT GVGLGQSRAK WFYLPEAKND FIFAIIGEEL
GLWGGALVIA TFLCLAYYGI RCALQSHNKY MSLLAASLTM GVIVQAFINI GYVIGLLPVT
GIQLPMLSAG GTSAIITLGS MGLLASCARY EPEAISAMQS YGRPFVDQVL RLKEPDLADI
EQPRPSRPRT KQAPRREPVV GRNAERRAEP RDGADGSVDR RSEKRRQSLR QQSRTRQTPP
TAGGRPERRR NS
//
