ID   FTSA_BUCAP              Reviewed;         418 AA.
AC   O51928;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN   Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; OrderedLocusNames=BUsg_207;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9425245; DOI=10.1007/s002849900284;
RA   Baumann L., Baumann P.;
RT   "Characterization of ftsZ, the cell division gene of Buchnera aphidicola
RT   (endosymbiont of aphids) and detection of the product.";
RL   Curr. Microbiol. 36:85-89(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC       Z ring. May serve as a membrane anchor for the Z ring.
CC       {ECO:0000255|HAMAP-Rule:MF_02033}.
CC   -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_02033}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02033}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02033}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02033}.
CC       Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to
CC       the membrane through a conserved C-terminal amphipathic helix.
CC       {ECO:0000255|HAMAP-Rule:MF_02033}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC       Rule:MF_02033}.
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DR   EMBL; AF012886; AAC46068.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67771.1; -; Genomic_DNA.
DR   RefSeq; WP_011053738.1; NC_004061.1.
DR   AlphaFoldDB; O51928; -.
DR   SMR; O51928; -.
DR   STRING; 198804.BUsg_207; -.
DR   EnsemblBacteria; AAM67771; AAM67771; BUsg_207.
DR   KEGG; bas:BUsg_207; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_3_2_6; -.
DR   OMA; DGIIRHT; -.
DR   OrthoDB; 1044637at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02033; FtsA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR003494; SHS2_FtsA.
DR   Pfam; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01174; ftsA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane.
FT   CHAIN           1..418
FT                   /note="Cell division protein FtsA"
FT                   /id="PRO_0000062732"
FT   CONFLICT        53
FT                   /note="N -> D (in Ref. 1; AAC46068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="Q -> P (in Ref. 1; AAC46068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="E -> D (in Ref. 1; AAC46068)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  46675 MW;  51D3A9FA723ABB46 CRC64;
     MIISKNRKLV VGLEIGTTKV VTLVGEVLTN GKIKIIGIGI CQSNGIDKGR INNLDAVISC
     IRESIHQAEI MANCQITSVY LSLSSKYINC QNEIGIVPIS EDEVTKEDIE NVIHTAKSVK
     ILNEHHILHV IPQEYSIDQQ SGIKNPIGLS GTRMQVRVHL ITCHQNMAKN IIKAVEKCDI
     KVDQVIFSGL ASSKAVLTED ECKLGVCMID IGGGTIDLIT YIDGSIQDSQ VIPYAGNIVT
     KDISYAFSTS YSDSEKIKIK YGSAIKLSPG TSKNIDLSSK YGNFQKNLQQ DTVIEVIESR
     YNELLHLINN RILYVQKKLY KEGRKYQLTG GIVLTGGAST ISFLTECAEK IFQKKIRIAK
     PLNISGLTDN VTEPHYSTVV GLLHYGKEFY FDDTNQKREI SFIEKWFQKI SNWFKKEF