ID   FTSW_BLOPB              Reviewed;         398 AA.
AC   Q493Q2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=BPEN_145;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40785.1; -; Genomic_DNA.
DR   RefSeq; WP_011282692.1; NC_007292.1.
DR   AlphaFoldDB; Q493Q2; -.
DR   SMR; Q493Q2; -.
DR   STRING; 291272.BPEN_145; -.
DR   EnsemblBacteria; AAZ40785; AAZ40785; BPEN_145.
DR   KEGG; bpn:BPEN_145; -.
DR   eggNOG; COG0772; Bacteria.
DR   HOGENOM; CLU_029243_1_1_6; -.
DR   OMA; KLWWSNL; -.
DR   BioCyc; CBLO291272:BPEN_RS00710-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007794; 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; IPR018365; Cell_cycle_FtsW-rel_CS.
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.
DR   PROSITE; PS00428; FTSW_RODA_SPOVE; 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; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..398
FT                   /note="Probable peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000415176"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        51..67
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        89..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        113..120
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        142..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        178..180
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        223..292
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        314..325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        347..354
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        376..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   398 AA;  45039 MW;  CB1A7102E59CD565 CRC64;
     MRLFKTKIIN RPLKLGKKKS SNIHVLYDRI FFWLLLGLIG IGFVIISSGS IPTGMRLAND
     PCYFIKRVIV YYSVTFLLSV IILKIPIIVW QNYSAIMLLC SCIMLITALI LNNSTNGASR
     WIMWGTLCIQ PAELSKLSFI CYLANYLERK SKEVCTKFWS ICKPIVIMII LAVLLLAQPD
     FGSIIILFIT TLSILFLFGA KLCQLILVFV FNIFLIIPLI VIKPYRIQRI LTFWDPWKDP
     FGNGYQLTQS LIAFGRGKCF GEGLGNSVLK LEYLPEAHTD FIFSILAEEL GYFGAILVLF
     MLFIIVLRAM IIGHRALNIN HRFSGILACS ISMWFGLQIF INVGTVSGIL PTKGLTLPFI
     SYGGSSFLIT VMASMQLLRI DFETRLSKNQ AFLKCTKI