ID A0A1I1PI26_9FLAO Unreviewed; 468 AA.
AC A0A1I1PI26;
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=SAMN05216297_104173 {ECO:0000313|EMBL:SFD09494.1};
OS Flavobacterium phragmitis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=739143 {ECO:0000313|EMBL:SFD09494.1, ECO:0000313|Proteomes:UP000199672};
RN [1] {ECO:0000313|EMBL:SFD09494.1, ECO:0000313|Proteomes:UP000199672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10370 {ECO:0000313|EMBL:SFD09494.1,
RC ECO:0000313|Proteomes:UP000199672};
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; FOMH01000004; SFD09494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1PI26; -.
DR STRING; 739143.SAMN05216297_104173; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000199672; 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; -; 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..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 468 AA; 51302 MW; 89A398D04CB4B052 CRC64;
MEKDNIAVGL DIGTTKIVAM IGKKNEYGKL EILGIGKSKS LGVARGVVNN ITQTIQSIQQ
AIIEAENNSG YKIKDVVVGI AGQHIRSIQH TDYISRNNPE EVIGENDIQL LIDQVNKLAM
LPGEEIIHVL PQEFKIDGQS EIKEPIGMYG GRLESSFHVV VGQASSIRNV GRCIQSSGIE
LSGLTLEPLA SADAVLSQEE KEAGVALIDI GGGTTDLAIF KDGIIRHTAV IPFGGNVITD
DIKEGCSIIE KQAELLKIKF GSAWPGENKD NEIVSIPGLR GREPKEISLK NLSKIIHARV
VEIVEQVFAE IKAYGHEDPR KKLIAGIVLT GGGAQLKHIK QLVEYITGMD TRIGYPNEHL
AGNSGEEISS PLFATAVGLV MNSIENSSQS AVRMELVNEQ PKVVYRNAPP VQRYEVEENY
VEKVETIEET REVVSRKASK DESTETKIRR SFFDRYVDKI KEFLDNAE
//
