ID A0A0G2AM58_9BACT Unreviewed; 410 AA.
AC A0A0G2AM58;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, 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=UY78_C0004G0009 {ECO:0000313|EMBL:KKW33724.1};
OS Parcubacteria group bacterium GW2011_GWA1_53_13.
OC Bacteria.
OX NCBI_TaxID=1618800 {ECO:0000313|EMBL:KKW33724.1, ECO:0000313|Proteomes:UP000034721};
RN [1] {ECO:0000313|EMBL:KKW33724.1, ECO:0000313|Proteomes:UP000034721}
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:KKW33724.1}.
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DR EMBL; LCRJ01000004; KKW33724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2AM58; -.
DR PATRIC; fig|1618800.3.peg.96; -.
DR Proteomes; UP000034721; 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 5..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 410 AA; 44144 MW; 9BCD3F72B0B48E08 CRC64;
MGRIITALDI GTSTIHTIVA ERRKRGEGLR ILGVGVSPSL GVRRGAIVDI EEAGAAIRRS
VDDAERASSA SIKQVWLAVG GAAVSVASSR GVVAVSRADG EISPEDVKRA VSAAQSFLPR
QPNREVIHMV PRDFKVDNES GVKDPVGMHG VRLEVDTLII ECASPFLKNI SKTLEHVGLT
VEDFVFSPLA TAEVVLTKRQ KELGVMLLDI GGGTASFIVF EEGVPMQAGV LPVGGGHITN
DIAIGFRTHI DVAEAIKLAY GSCLPRELPK RESIRLADFV EGESAIYSRR ELAEIIEARM
GDVFELLHRE LKKINRIQLL PAGVVIVGGS SLLPGLVDLA KQEMRLPIER GALQEFTAVA
DDITAPSLAP ALGVLMWADR MIHGGGSAWS KDLPGFSENR WMRWLRSLIP
//
