ID A0A1J5F6A5_9BACT Unreviewed; 411 AA.
AC A0A1J5F6A5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=AUK10_02880 {ECO:0000313|EMBL:OIP53066.1};
OS Candidatus Gracilibacteria bacterium CG2_30_37_12.
OC Bacteria; Candidatus Gracilibacteria.
OX NCBI_TaxID=1805211 {ECO:0000313|EMBL:OIP53066.1, ECO:0000313|Proteomes:UP000182482};
RN [1] {ECO:0000313|EMBL:OIP53066.1, ECO:0000313|Proteomes:UP000182482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_37_12 {ECO:0000313|EMBL:OIP53066.1};
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:OIP53066.1}.
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DR EMBL; MNYO01000090; OIP53066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5F6A5; -.
DR Proteomes; UP000182482; 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; 3.30.420.40; -; 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..193
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 411 AA; 44333 MW; 8AC6BBBCD4DBC2C0 CRC64;
MVSGEVFTAI DIGTAKIKTV IATFTEDKKL RVLGVGIAKS NGIRKGNIID MDEFKKNIDD
SLSEAERMTG EQVSAIYLSL SGTNIEVVTN NGIISVPHGE VSTEDVNRVL DMSQNGVDLM
NKVVLKVIPE AFTLDMESGV KNPVGMSAKK LEVRSHIFCI SSNILSNIKK GIYDVGVDIL
DIYPNVLAAP EAVLSKRQKE LGVVCIDIGA STTDVAVYEE GSLIFATVIP IGGEHVTSDI
ALGARVSIDT AEKLKIEYGS IGFCKDEKAK DDEIDLAKIS KNETTTISRK YLSEIIRARY
SEIFYYVNNE LKKIGRDGML PEGAVISGGG AKARDINELA KEVLRLPSMI GTPEDSDFIS
GTSIGDPMFA GIIGTLLLSQ KYGVTRSGFK FNLSFGGFLG SIKNALKKIM P
//