ID A0A1H2TWU1_9RHOB Unreviewed; 444 AA.
AC A0A1H2TWU1;
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=SAMN04488238_102200 {ECO:0000313|EMBL:SDW48178.1};
OS Roseicitreum antarcticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseicitreum.
OX NCBI_TaxID=564137 {ECO:0000313|EMBL:SDW48178.1, ECO:0000313|Proteomes:UP000198539};
RN [1] {ECO:0000313|EMBL:SDW48178.1, ECO:0000313|Proteomes:UP000198539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8894 {ECO:0000313|EMBL:SDW48178.1,
RC ECO:0000313|Proteomes:UP000198539};
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; FNOM01000002; SDW48178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2TWU1; -.
DR STRING; 564137.SAMN04488238_102200; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000198539; 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:UP000198539};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..225
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 444 AA; 47963 MW; EB09F79A9AAEAB4D CRC64;
MQDLYQSQRA MRQMRRLAMQ RGVIGIVDVG TFKIAALVLK FDPTAAPRDG AGVGGMAGQA
GFRVIGARTT RSRGVRYGEI STMNETERAL RTALQAAQKM AQVRVDHAIL CFSGGGVRSY
GLAGDVELED MTVGSDDIAR VLAACDVPDI GVGRDVLHAQ PVNFALDHRT GLSDPRGQTG
TRLACDMHML TVNTGVIQNL VNCMKRCDVE LAGLASSAYM AGVSSLVEDE QELGAACIDM
GAGSTGISIF IKKHLIFSDT VPMGGDHVTG DIAQGLHVPV ATAERIKTLH GGVHATGMDD
REMIEIGADS GDWEKDRRTV SRAELIGIMR PRFEEILEEV RARLDAAGFD HLPSQQIVLT
GGASQTPGID SLAARILGQQ LRLGRPMRVR GLPQDLTGPA FAGVVGLSLF AAHPQDEWWD
FDIPVDHYPA RSLKRAVRWF RDNW
//
