ID A0A1F5QAB2_9BACT Unreviewed; 415 AA.
AC A0A1F5QAB2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=A3J05_04700 {ECO:0000313|EMBL:OGE99046.1};
OS Candidatus Doudnabacteria bacterium RIFCSPLOWO2_02_FULL_48_13.
OC Bacteria; Candidatus Doudnabacteria.
OX NCBI_TaxID=1817845 {ECO:0000313|EMBL:OGE99046.1, ECO:0000313|Proteomes:UP000177235};
RN [1] {ECO:0000313|EMBL:OGE99046.1, ECO:0000313|Proteomes:UP000177235}
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|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to
CC the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC Rule:MF_02033, 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:OGE99046.1}.
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DR EMBL; MFFF01000023; OGE99046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5QAB2; -.
DR Proteomes; UP000177235; Unassembled WGS sequence.
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 Gene3D; 3.30.1490.110; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02033; FtsA; 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|HAMAP-
KW Rule:MF_02033};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033}.
FT DOMAIN 7..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 415 AA; 44124 MW; 7D1895344FB7529D CRC64;
MSSEQILVGL DIGTTTIRVV VGKKENPGTP PSIIGVGEAK ASGIRKGVIV DIEEAVSSIS
KALEKAERMT GIPTQHAVVS VGGAHVVSLE SHGVIAVARA DGEITENDVV RVIDAAQAIQ
VPTNREILHV IPKDFTVDGQ TGIKDPVGMT GIRLEVDAQI IEASIPFIKN LTKCVIQAGI
DIDDLVLAPL ASAQAVLTKR QKELGVVLIE LGGGTTGLVA FEESELLHTN ILAVGSDHIT
NDIAIGLRTS VDVADTVKLE YGRAMPTAVK KDEVINLSKI DKNEEGQVSR LHLTEIIQAR
LEEIFSMVNK ELKAAGRDGQ LPAGAVLTGG GAKLQGIVEL AKKELRLPVQ IGYPLNISTI
IDRVDDPAYA TAVGLVLWAD EYLASDKAGM GRFASKILQN ASIDKIRKFF KQFLP
//
