ID A0A1G2LBP7_9BACT Unreviewed; 408 AA.
AC A0A1G2LBP7;
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=A3B37_03280 {ECO:0000313|EMBL:OHA08229.1};
OS Candidatus Sungbacteria bacterium RIFCSPLOWO2_01_FULL_59_16.
OC Bacteria; Candidatus Sungbacteria.
OX NCBI_TaxID=1802280 {ECO:0000313|EMBL:OHA08229.1, ECO:0000313|Proteomes:UP000176705};
RN [1] {ECO:0000313|EMBL:OHA08229.1, ECO:0000313|Proteomes:UP000176705}
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:OHA08229.1}.
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DR EMBL; MHQS01000021; OHA08229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2LBP7; -.
DR STRING; 1802280.A3B37_03280; -.
DR Proteomes; UP000176705; 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..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 408 AA; 42939 MW; 14AE74746AA51BB7 CRC64;
MRNISVGIDI GTTTVTTLII EEGRNREVRI VGAGRTPSAG MRRGVVADVD AAAQAIHASV
LEAGRAAGVT VRSGNLGIGG AHLGIFSTRG VVAVSRADGE ITDSDTDRAL QAAEGFISKN
PNREIIHIIP RGFKIDGQGG LANPVGLVGM KLEVEALVID GAKQALANIV RACELAGIAI
DDWAANIIAA SNVLLSREQK ELGVMLLDLG AGTSDYAVFE EGRLLDAGSI PIGGMHITSD
IAIGFRTTIA AAEAIKVRHA QALAEGRLGK RDVIALGDFT SGDPSAYATR DLIDIVTARL
ADIFELSNKA LKRIGRSGLL PAGVVLAGGV AELPAIRELA RREMKLPAEV VRTIAGEEFE
GDIPSNLAVP LGLALWTGED RGILGYRRRR SWNGFPEAMK RIFRAFIP
//
