ID A0A1G2G5S3_9BACT Unreviewed; 409 AA.
AC A0A1G2G5S3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
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=A2756_00890 {ECO:0000313|EMBL:OGZ45557.1};
OS Candidatus Ryanbacteria bacterium RIFCSPHIGHO2_01_FULL_48_27.
OC Bacteria; Candidatus Ryanbacteria.
OX NCBI_TaxID=1802115 {ECO:0000313|EMBL:OGZ45557.1, ECO:0000313|Proteomes:UP000177785};
RN [1] {ECO:0000313|EMBL:OGZ45557.1, ECO:0000313|Proteomes:UP000177785}
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:OGZ45557.1}.
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DR EMBL; MHNL01000006; OGZ45557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2G5S3; -.
DR STRING; 1802115.A2756_00890; -.
DR Proteomes; UP000177785; 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 6..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 409 AA; 43330 MW; BA35CA2CA6DF9A0F CRC64;
MQRRIITGLD VGTTSVQVVV ADQKSEGGLE ILGFGRALSE GMRRGNVVDT HDVASSIRRA
VEDAERATGV PIEHAYVGFS GVGLGITATK GVVAVSRADG EISEADVDRV LANARAALPQ
LPNREVIHEI PSRYAVDKEM NIKNPVGMIG NRLEAQVLFI SAFTPYLKTL VKSVELAGLA
VDDIVASPLA AARAVLSKHQ KEIGVMTLDL GGGSASISVF EEGGLVSTGV FPVGSAHVTH
DIAIGFQTPL EVAERIKLEH GTLAAQSVGK RDTVRLADYI EGEATAISRR DLAEIIEARF
KDIFELVDKH LKKIGRSGLL PSGVVITGGG AGLPGIADFA KRELRLPAIV GTPVGISGSH
ENIQDPSWSV ALGLCLLGYD ETKTGSFKTA SVWQKILKRV GDWARPFIP
//
