ID A0A1I0Q202_9RHOB Unreviewed; 444 AA.
AC A0A1I0Q202;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, 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=SAMN04488515_1612 {ECO:0000313|EMBL:SEW20987.1};
OS Cognatiyoonia koreensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=364200 {ECO:0000313|EMBL:SEW20987.1, ECO:0000313|Proteomes:UP000199167};
RN [1] {ECO:0000313|EMBL:SEW20987.1, ECO:0000313|Proteomes:UP000199167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17925 {ECO:0000313|EMBL:SEW20987.1,
RC ECO:0000313|Proteomes:UP000199167};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOIZ01000001; SEW20987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Q202; -.
DR STRING; 364200.SAMN04488515_1612; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000199167; 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; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199167}.
FT DOMAIN 24..225
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 444 AA; 48047 MW; 77E901ECE0F9A7AD CRC64;
MRDLYESQRA MRNMRKAAMQ RGVIAILDVG TSKIACLVLR FDGPEKFGDN DVIGSLAGQS
TFRVIGAATT RSRGVRFGEV DAMQETERAI RTAVQAAQKM ANVRVDHVIA TLSGARPKSY
GLDGSVDIEG GMVTDMDIGR VMAACDVPDY GADREVLHAQ PVNFALDHRS GMADPRGQIG
NQLNTDMHML TVDAIALQNL YFCIKRCDLE LAGLASSAYV SGISSLVEDE QELGAACIDM
GGGSTGISVF MKKHMIYADA VRMGGEHVTG DISMGLQVPT ATAERIKTFY GGVVATGMDD
REMIEIGGNT GDWEHDRRTV SRAELIGIMR PRVEEILEEV RVRLDAAGFE HLPSQQIVLT
GGASQIPGLD GLASKILGQQ VRLGRPLRVQ GLPQAATGPA FSGAVGATLF AANPQDEWWD
FEIPAETYPA RSLKRAVKWF KDNW
//
