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Database: UniProt
Entry: A0A101C8X4_9FLAO
LinkDB: A0A101C8X4_9FLAO
Original site: A0A101C8X4_9FLAO 
ID   A0A101C8X4_9FLAO        Unreviewed;       412 AA.
AC   A0A101C8X4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=AR685_09505 {ECO:0000313|EMBL:KUJ51858.1};
OS   Chryseobacterium sp. JAH.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1742858 {ECO:0000313|EMBL:KUJ51858.1, ECO:0000313|Proteomes:UP000054026};
RN   [1] {ECO:0000313|EMBL:KUJ51858.1, ECO:0000313|Proteomes:UP000054026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAH {ECO:0000313|EMBL:KUJ51858.1,
RC   ECO:0000313|Proteomes:UP000054026};
RA   Newman J.D., Frantz D.C., Miller J.R.;
RT   "Genome Sequence of Chryseobacterium sp. JAH.";
RL   Submitted (OCT-2015) 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:KUJ51858.1}.
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DR   EMBL; LMAH01000003; KUJ51858.1; -; Genomic_DNA.
DR   RefSeq; WP_047443419.1; NZ_LMAH01000003.1.
DR   AlphaFoldDB; A0A101C8X4; -.
DR   STRING; 1742858.AR685_09505; -.
DR   OrthoDB; 9812661at2; -.
DR   Proteomes; UP000054026; 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:KUJ51858.1};
KW   Cell division {ECO:0000313|EMBL:KUJ51858.1};
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   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        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..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   412 AA;  45401 MW;  B5F412FEE4CD2660 CRC64;
     MNDQYTENKF EYLKGDKVLW MVIIVISIFS IFPVYSASSN LEYIVNNGTT TGHVMKHMFF
     VVLGLVIMRF VGVVKYEYIG KLSSILLGLM ILLLVVTMFT GQTIDGASAS RWLKIPGTPI
     SFQPSSFAFL MLIIYLCRYL TKKITRERTV WENIGFIFGP ILLVFVLVAK DNGSTALMIL
     MVSVIVLVIG QLHWKYIAGF ISSAFIAIVL FLLIALNTNM IGGNRVHTWM SRIETFTSSK
     AKTADVDDES VKAKNYQVMQ AKAAIVHGGI TGMGPGKSAL KQMLPQSASD FIFAVIVEEY
     GAIGAAFLIS MYLIMIIRIV MIASKMPAFF GSLLVLSLGV MIFIQLAVNI AVAVNLIPVT
     GQPLPLISYG GTSMLVTYMQ LGIILNVSSR IQIYDEEGMG KKQSIVEIND IA
//
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