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Database: UniProt
Entry: A0A1H4D694_9GAMM
LinkDB: A0A1H4D694_9GAMM
Original site: A0A1H4D694_9GAMM 
ID   A0A1H4D694_9GAMM        Unreviewed;       409 AA.
AC   A0A1H4D694;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00913};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
GN   Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913};
GN   ORFNames=SAMN05660964_02171 {ECO:0000313|EMBL:SEA68137.1};
OS   Thiothrix caldifontis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA68137.1, ECO:0000313|Proteomes:UP000199397};
RN   [1] {ECO:0000313|EMBL:SEA68137.1, ECO:0000313|Proteomes:UP000199397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA68137.1,
RC   ECO:0000313|Proteomes:UP000199397};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988, ECO:0000256|HAMAP-
CC         Rule:MF_00913};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00913}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=Localizes to the
CC       division septum. {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|ARBA:ARBA00038053, ECO:0000256|HAMAP-Rule:MF_00913}.
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DR   EMBL; FNQP01000011; SEA68137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4D694; -.
DR   STRING; 525918.SAMN05660964_02171; -.
DR   OrthoDB; 9768187at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199397; Unassembled WGS sequence.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   NCBIfam; TIGR02614; ftsW; 1.
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:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00913};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00913}.
FT   TRANSMEM        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        63..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        91..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        120..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        156..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        179..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        203..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        287..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        320..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        354..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ   SEQUENCE   409 AA;  44988 MW;  D7E0EFB729FD2334 CRC64;
     MIKLPSLMLD TPTDNFWSRY VDRDLLIALL AIIGIGIVML ASASLWVAEK QYNDPYFYLQ
     RQAFYLAIGV VLALGMYQIR VDFWQQLGVR LLPLVLVLLV LVLIPGIGKE VNGSRRWLNL
     GFMAIQVSEL AKLIMLLYLS GYLIRHGKSL ATSPSYQPLL IPLVVLGVTG GLLLLEPDFG
     STIVIFVTGL SLLFLGGVPL QRLGILIGGA ILVMIPVSMM GYRGARWDAL MNPWAHEADK
     GYQTVHALMA IGDGGWFGNG LGGGIQKLFY LPEAHNDFIF SILAEEFGFI GMLVVLSLYG
     WLVLRAFVIG FQADKAGKHF GAYVAYGIGF WMGFQVILHI GVNLAVLPPK GLTLPLMSYG
     GSSLLVTLMA MALLMRVHRE TQLVQFGLPE VRAPKPPKAR AIRRTTRGE
//
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