ID A0A0G1LF31_9BACT Unreviewed; 402 AA.
AC A0A0G1LF31;
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=UW62_C0028G0004 {ECO:0000313|EMBL:KKT67277.1};
OS Candidatus Collierbacteria bacterium GW2011_GWB1_44_35.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618383 {ECO:0000313|EMBL:KKT67277.1, ECO:0000313|Proteomes:UP000034604};
RN [1] {ECO:0000313|EMBL:KKT67277.1, ECO:0000313|Proteomes:UP000034604}
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:KKT67277.1}.
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DR EMBL; LCJA01000028; KKT67277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LF31; -.
DR PATRIC; fig|1618383.3.peg.292; -.
DR Proteomes; UP000034604; 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; -; 1.
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 9..175
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 402 AA; 42964 MW; DF2871F26710BF92 CRC64;
MFNHCPFSRR RKNKSCWGCY CTEKKGQIVN IEEAVGSISD CVEAAERMAG FNIDQAYVSI
NGDHIQSQNS QGLVAITESE GEIAEDDIYR VIEAARAISL PTAREIIHVL PREFIVDSQR
GIKDPTGMSG VRLETEAHLV TGLSPAIKNV SRCVSDLGIN VAGQVFTGLA SSHSVLTETE
KELGVILADI GAGTTSISVF IEGACSYSAV IPVGARKITD DIAIGLTSSI DTAERIKHYL
SKGKGERDGD KPADEIDFEK LGIREDHLKT GSRKAITEGI IRPRLNEIFS LLRDVLKKSG
FEGQTPAGVV LTGGGAMTAG ALESCRRVMQ LPPRIGVPSG LSGIVDEVST PIYAASVGLI
LYGYKQKPQN SAGGVKLSGI FKKVPGKDMA GKALEFIKSF LP
//