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Database: UniProt
Entry: A0A1G1LUF2_9BACT
LinkDB: A0A1G1LUF2_9BACT
Original site: A0A1G1LUF2_9BACT 
ID   A0A1G1LUF2_9BACT        Unreviewed;       410 AA.
AC   A0A1G1LUF2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Cell division protein FtsA {ECO:0000256|PIRNR:PIRNR003101};
GN   ORFNames=A2Z88_11240 {ECO:0000313|EMBL:OGX08797.1};
OS   Omnitrophica WOR_2 bacterium GWA2_47_8.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801840 {ECO:0000313|EMBL:OGX08797.1, ECO:0000313|Proteomes:UP000178620};
RN   [1] {ECO:0000313|EMBL:OGX08797.1, ECO:0000313|Proteomes:UP000178620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:0000256|PIRNR:PIRNR003101}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000256|PIRNR:PIRNR003101}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family.
CC       {ECO:0000256|PIRNR:PIRNR003101}.
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:OGX08797.1}.
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DR   EMBL; MHFY01000014; OGX08797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1LUF2; -.
DR   STRING; 1801840.A2Z88_11240; -.
DR   Proteomes; UP000178620; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.110; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR003494; SHS2_FtsA.
DR   NCBIfam; TIGR01174; ftsA; 1.
DR   PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR   PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR   Pfam; PF14450; FtsA; 1.
DR   Pfam; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR003101};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   ECO:0000256|PIRNR:PIRNR003101};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          10..198
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   410 AA;  45570 MW;  1861297F0D90BB37 CRC64;
     MLGKFGERYI CGLDLGSCHT KASLLKVTES SEDLIGAFEL RTRGFREASV SDLSELTECV
     HQTIEGLTKN TAIKLKELYL GVGGELVESR HNTTVIPLVE RGSKIIGGYD IKRINKQARF
     LGLKVDEEVL HDFPQYYKVD DVNTALNPLG LFGRKLEVNS LLLVSNLTKL RNITKAVNQA
     GYEVGGIYFT SYGALSVCSK NYTKDDIFIL VDIGWKVTDI LLITHSQIKS LIKVPLGGHH
     ITEGLAQSLC LSYELAEEIK KTYAIALVND PRNEEEILVK KEANYDPIKR KEIAVAIQPA
     IQEFLQALKE RLVATNMLEH INKGIVMVGG GALLPGLMER LEEEIRLPVN SAKMTVGTKT
     ATLSPVFAPV MGIAKLGIQK VWGEDFASNG NTRRMDLLLT RLRDLYQEYF
//
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