ID A0A0G0DD63_9BACT Unreviewed; 418 AA.
AC A0A0G0DD63;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=UR43_C0007G0111 {ECO:0000313|EMBL:KKP53187.1};
OS candidate division TM6 bacterium GW2011_GWF2_33_332.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53187.1, ECO:0000313|Proteomes:UP000034634};
RN [1] {ECO:0000313|EMBL:KKP53187.1, ECO:0000313|Proteomes:UP000034634}
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:KKP53187.1}.
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DR EMBL; LBPE01000007; KKP53187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DD63; -.
DR PATRIC; fig|1619080.3.peg.1009; -.
DR Proteomes; UP000034634; 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 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 418 AA; 45465 MW; 93EC54698D2BF6B2 CRC64;
MRKKLLNKHW VGIDVGTSKI CVLIAGLDHN GNIEILGIGQ HPSVGLKKGV VVDINSTIKS
IKKAVESAEN MAGIKVDSAV VGISGGHIQA INSQGVVAIK HGDVSQYDID RVIDAAKAVA
IPQDREILHI LPQYFKIDGQ ELIKDSMGMK GIRLEAQVHI ITGSISSASN LIKCCEDAGI
SVEDIVLETI ASADATLSED ERELGVGMVD IGAGTSDFAI YKDGKILHSK VVPVAGNHFT
RDLAIAFRIP LETAEFIKRK YGAVSYKNVL GLIDNAIKVD VGPDLVKQIK TTDICDILMP
RAEEMLEFIF DEIIKFNLKR FMPFGLVLTG GGSMLSGMKE LAENMFGMPV RIGFPQNNIK
TSGLEFVPDL LKSPIYSTGY GLLLYASKDK DLTLAKSMNE KGASKVFKRM KSWIYDLF
//
