ID A0A1Z4VUF1_9GAMM Unreviewed; 410 AA.
AC A0A1Z4VUF1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=FOKN1_2662 {ECO:0000313|EMBL:BAZ95032.1};
OS Thiohalobacter thiocyanaticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thiohalobacter.
OX NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ95032.1, ECO:0000313|Proteomes:UP000218765};
RN [1] {ECO:0000313|EMBL:BAZ95032.1, ECO:0000313|Proteomes:UP000218765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ95032.1,
RC ECO:0000313|Proteomes:UP000218765};
RA Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
RL Submitted (MAY-2017) 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; AP018052; BAZ95032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4VUF1; -.
DR KEGG; ttc:FOKN1_2662; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000218765; Chromosome.
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; 2.
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:UP000218765}.
FT DOMAIN 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 410 AA; 44171 MW; 6BF4BECD9615AE8A CRC64;
MTKRSEKNMI VGLDIGTSKV VAIVGEVLPE GGIEIIGIGS HPSRGMKKGV VVNIESTVHS
IQRAIEEAEL MAGCQIHSVY AGIAGSHIRS LNSHGIVAIR DKEVTPGDVE RVIDAARAVA
IPADQKILHI LPQEFIIDNQ EGIKEPVGMS GVRLEAKVHL VTGAVSAAQN IIKCVRRCGL
EVDDIILEQL ASSYSVLTED EKELGVCLVD VGGGTTDMAV FTEGSIRHTS VIPIAGDQVT
NDIAVALRTP TQHAEEIKIK YACALTQLAS SDDTIEVPSV GDRPARRLAR HTLAEVVEPR
YEELLTLVQS ELRRSGFEDL VAAGIVLTGG SSKMEGLVDL AEEVFHMPVR LGMPQYVAGL
ADVVRNPIYA TGVGLLLFGN QNQSHLNLDI QGRGFRGVWD RMKSWFQGNF
//