ID A0A1G7GF26_9FLAO Unreviewed; 446 AA.
AC A0A1G7GF26;
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=SAMN05421855_10391 {ECO:0000313|EMBL:SDE86619.1};
OS Ulvibacter litoralis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=227084 {ECO:0000313|EMBL:SDE86619.1, ECO:0000313|Proteomes:UP000199321};
RN [1] {ECO:0000313|EMBL:SDE86619.1, ECO:0000313|Proteomes:UP000199321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16195 {ECO:0000313|EMBL:SDE86619.1,
RC ECO:0000313|Proteomes:UP000199321};
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; FNBA01000003; SDE86619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7GF26; -.
DR STRING; 227084.SAMN05421855_10391; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000199321; 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:UP000199321}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 446 AA; 48914 MW; 43798DD02AECC518 CRC64;
MENENIAVGL DIGTTKIVAM IGKTNEYGKM EVLGIGKSKS LGVHRGVVNN ITQTIQSIQQ
AVQDAETSSG MKIHDVVVGI AGQHIRSLQH SDYITRANSD EVIDESDIDR LCNQVHKLVM
LPGEEILHVL PQDFKVDGQA EVKEPIGMYG ARLEANFHVV VGQVSSIRNV GRCIKSAGLE
LSGITLEPLA SAQAVLSQEE KEAGVALIDI GGGTSDLAIF KDGIIRHTAV IPFGGNVITE
DIKEGCSIIE KQAELLKIKF GSAWPGENKD NEIVSIPGLR GREPKEITLK NLSKIIHARV
VEIIEQIYLE IKNYGHEEQK KKLIAGIVLT GGGAQLQHLK QLVEYITGMD TRIGYPNEHL
AGDSDSETTS PLYATAVGLV LNSLQNKEKE KTSARKSVLH EEEINAETVS EVAEEEEDLV
EEKPKETRRF FDKWAEKFKE FLDNAE
//