ID A0A1J5FRA7_9BACT Unreviewed; 430 AA.
AC A0A1J5FRA7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
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=AUK12_00920 {ECO:0000313|EMBL:OIP58262.1};
OS Candidatus Levybacteria bacterium CG2_30_37_29.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1805237 {ECO:0000313|EMBL:OIP58262.1, ECO:0000313|Proteomes:UP000182355};
RN [1] {ECO:0000313|EMBL:OIP58262.1, ECO:0000313|Proteomes:UP000182355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_37_29 {ECO:0000313|EMBL:OIP58262.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIP58262.1}.
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DR EMBL; MNYS01000002; OIP58262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FRA7; -.
DR STRING; 1805237.AUK12_00920; -.
DR Proteomes; UP000182355; 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..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 430 AA; 46012 MW; 9F70DA1E48ACCD02 CRC64;
MRDNQIVVGV DIGSSKIATV IGQIQQDSVN ILGVTEIPSK GIKKGQIVDI VEAAGVINSS
LDASERMAGY AVDHVFVSLS GVHIQSQNSK GIVAISNPEG EIFQPDVERV LEAAGAVSMP
STTTVLHVLP KTFTVDGEPS IKDPIGMTGV RLEVDTHIIS ANSVSVKNVQ RVLEQEAGVG
INALVFSGFA SSLAVLTETE KELGVVLVDI GAGITNICIF VEGALSYSGV IPIGARHITN
DLAIGLRISL ESAEKIKLYL SKKYGRRQRA VRVEGDENAD ELDLGELHLI EDLKKVSQKT
LVDGIIRPRL NELFTMIGIE LKKSGFATQT PAGVVITGGG ARTVGAEEAA KRMLSMPVRV
GYPQNISGLI DDVENPSFAT AVGLLIFGRD FKSHESGAIF NNLFSSIKFK PLNNLVSRIK
KIFKNFTPRF
//
