ID A0A1B9DXR6_9FLAO Unreviewed; 461 AA.
AC A0A1B9DXR6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=LPBF_10840 {ECO:0000313|EMBL:OCB74476.1};
OS Flavobacterium crassostreae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1763534 {ECO:0000313|EMBL:OCB74476.1, ECO:0000313|Proteomes:UP000093510};
RN [1] {ECO:0000313|EMBL:OCB74476.1, ECO:0000313|Proteomes:UP000093510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0076 {ECO:0000313|EMBL:OCB74476.1,
RC ECO:0000313|Proteomes:UP000093510};
RA Ploux O.;
RL Submitted (MAR-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}.
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:OCB74476.1}.
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DR EMBL; LVEP01000038; OCB74476.1; -; Genomic_DNA.
DR RefSeq; WP_066336273.1; NZ_LVEP01000038.1.
DR AlphaFoldDB; A0A1B9DXR6; -.
DR STRING; 1763534.GCA_001831475_00131; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000093510; 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 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; 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:UP000093510}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50187 MW; 4342EC089B9A8083 CRC64;
MEKENIAVGL DIGTTKIVAM IGKKNEYGKL EILGVGKSKS LGVARGVVNN ITQTIQSIQQ
ALQEAEINSG YKIKDVVVGI AGQHIRSIQH TDYISRNNPE EVIGGADIQL LIDQVNKLAM
LPGEEIIHVL PQEFKIDGQS EIKEPIGMYG GRLEASFHVV VGQASSIRNV GRCIQSSGIE
LSGLTLEPLA SSDAVLSQEE KEAGVALIDI GGGTTDLAIF KDGIIRHTAV IPFGGNVISD
DIKEGCSIIE KQAELLKIKF GSAWPGENKD NEIVSIPGLR GREPKEISLK NLSKIIHARV
VEIVEQVFTE IKAYGHEDPR KKLIAGIVLT GGGAELKHIK QLVEYITGMD TRIGYPNEHL
AGDSDEQFSS PLYATAVGLV MNSIENKTNS AVRLDAIVPP KPVYQAPVTP RETLAHREEQ
EMAAQENDNN AKKEESTGDK IKRSFFDRYV DKIKDFLDNA E
//