ID A0A0G0S673_9BACT Unreviewed; 420 AA.
AC A0A0G0S673;
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=UT50_C0011G0004 {ECO:0000313|EMBL:KKR21187.1};
OS Candidatus Moranbacteria bacterium GW2011_GWA2_39_41.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618695 {ECO:0000313|EMBL:KKR21187.1, ECO:0000313|Proteomes:UP000034867};
RN [1] {ECO:0000313|EMBL:KKR21187.1, ECO:0000313|Proteomes:UP000034867}
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:KKR21187.1}.
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DR EMBL; LBXA01000011; KKR21187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0S673; -.
DR PATRIC; fig|1618695.3.peg.402; -.
DR Proteomes; UP000034867; 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 420 AA; 44666 MW; 1A3BE3F193A5D674 CRC64;
MASRDIIVGI DIGSSSVRTV IARIFPEEEK PRIIGVGSAA STGVRKGVIV DLEEATKSIN
ESVEQAERTS GVAVSQAVVS IGGNHITSQH SKGVIAVGRA DGEVAEDDIE RVINAAQAIS
IPPNKEILHI IPETYSLDDN KNIKDPFGMN GVRLEVDAMI VEGSTPFIKN LTKCFEQAGI
AISDFVLAPL AATKATLTKR QKELGVVLVD IGGGTTSMAV FEENDLLHTT ILPIGGNHIT
NDIAIGLRTS IDVAERVKLE YGNALPREIG KREEINLAEL DSSEEGIVSR YHVAEIIEAR
LEEIFLLVNK ELKMIGREKL LPAGVILTGG TAKLPGAVDL AKNILGLPAQ TGFPMQLGGL
IDKVDDPAFV TVIGLILWGL ENDSSARGGM MLKNKLTGSI SNGMSGGIDG MKKWIGKFLP
//
