ID A0A0G1KF75_9BACT Unreviewed; 427 AA.
AC A0A0G1KF75;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
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=UW78_C0002G0021 {ECO:0000313|EMBL:KKT82140.1};
OS Candidatus Azambacteria bacterium GW2011_GWA1_44_9.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618610 {ECO:0000313|EMBL:KKT82140.1, ECO:0000313|Proteomes:UP000034595};
RN [1] {ECO:0000313|EMBL:KKT82140.1, ECO:0000313|Proteomes:UP000034595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT82140.1}.
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DR EMBL; LCJQ01000002; KKT82140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KF75; -.
DR PATRIC; fig|1618610.3.peg.97; -.
DR Proteomes; UP000034595; 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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 427 AA; 44483 MW; B17E5DB4B98D5DA2 CRC64;
MAKPKVLAGI DIGSAKIASL IAQYDELEDK LSISGVGSVP SKGVRKGQIV DIDEAASSII
ESVEQAERMA GYNLDQAVLT IGGGHVDSRN SNGVVAVADP GGEISSQDIE RVIEAARAVS
LPEAREILHV IPKEYRVDGE TQVKDPEGMS GVRLEVETHL ITGSTTAVKN VQKSVSEVGV
TPQGLVFSGL AAATSVLSDT ERELGVVLVD VGAGTTSIIV YIEGSIAHSS VLPIGSKNVT
NDIAAGLRVS LDSAEKIKIM LGDRRKKGKA GEEDNDELDL KSYGVEEGDR KVSEKTLVEG
IIKPRLNEVF TMVGMNLADS GVAGKTPSGV VITGGGALCV GAAESARRML SLPTRVGTPK
GVVGLVEEIS SPVFAAAVGL LIYSSRNPSS REMSWSPANI ISKTFRGGLP VRGLVGRASD
LVKKILP
//
