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Database: UniProt
Entry: A0A426RSE2_9SPHN
LinkDB: A0A426RSE2_9SPHN
Original site: A0A426RSE2_9SPHN 
ID   A0A426RSE2_9SPHN        Unreviewed;       406 AA.
AC   A0A426RSE2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 37.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|ARBA:ARBA00041185};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
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=D7D48_03375 {ECO:0000313|EMBL:RRQ51930.1};
OS   Sphingorhabdus wooponensis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=940136 {ECO:0000313|EMBL:RRQ51930.1, ECO:0000313|Proteomes:UP000268553};
RN   [1] {ECO:0000313|EMBL:RRQ51930.1, ECO:0000313|Proteomes:UP000268553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03SU3-P {ECO:0000313|EMBL:RRQ51930.1,
RC   ECO:0000313|Proteomes:UP000268553};
RA   Kim S.-J., Jung G.-Y.;
RL   Submitted (DEC-2018) 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=2.4.99.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00049902};
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:RRQ51930.1}.
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DR   EMBL; RWJI01000001; RRQ51930.1; -; Genomic_DNA.
DR   RefSeq; WP_125229946.1; NZ_RWJI01000001.1.
DR   AlphaFoldDB; A0A426RSE2; -.
DR   OrthoDB; 9768187at2; -.
DR   Proteomes; UP000268553; Unassembled WGS sequence.
DR   GO; GO:0032153; C:cell division site; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:TreeGrafter.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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:RRQ51930.1};
KW   Cell division {ECO:0000313|EMBL:RRQ51930.1};
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:UP000268553};
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        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        330..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   406 AA;  44307 MW;  D0B2A48F97C9E1C6 CRC64;
     MSDNTEAPWV LAAKTGKIGF ANRLGRGDRS PLGVWFWELD RVLLSLMMVL IAIGLLAVAA
     ASPAGAQRLS SSTTELSSLH FFYRQLIFVG IGVPIMLAIS MCPREKARRF AVYGFCIFFV
     LLALVPILGR EVNGSQRWIG PGFAGLQPSE FLKPFFAVMM AWIISWRLKD PGLPVLVLTS
     IATGLVCLFL LLQPDLGQTI LFMGTWFALM MVAGVPASRL WFLVISGVVF ILLAYNFYPV
     ATQRIDAWIF GTEGLTHDKM ALATLTNGGF IGLGPGLGIK KYSLPEGHTD YIFSVIGEEF
     GLLSCMAIAI LYFAILVRII IRLLDEKDQF VVMAVTGLGA QFCGQAMINI AVNLGVFPSK
     GMTLPFISYG GSSIIALSIT CGLILALTKR NPYLDRSLYM VKGHKP
//
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