ID A0A1T5DCL3_9FLAO Unreviewed; 451 AA.
AC A0A1T5DCL3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05660866_02826 {ECO:0000313|EMBL:SKB69454.1};
OS Maribacter arcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=561365 {ECO:0000313|EMBL:SKB69454.1, ECO:0000313|Proteomes:UP000190339};
RN [1] {ECO:0000313|EMBL:SKB69454.1, ECO:0000313|Proteomes:UP000190339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23546 {ECO:0000313|EMBL:SKB69454.1,
RC ECO:0000313|Proteomes:UP000190339};
RA Peterson S.W.;
RL Submitted (FEB-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; FUYL01000009; SKB69454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5DCL3; -.
DR STRING; 561365.SAMN05660866_02826; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000190339; 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}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 451 AA; 49413 MW; E1A24C525F6244CE CRC64;
MEQTKYSVGL DIGTTKIVAI IGKENEYGKI EILGIGKSKS LGVHRGVVNN ITQTIKSIQQ
AVEEAEANSG LKIGSVVVGI AGQHIRSLQH SDYITRKDSE EVINEEDLDI LINQVHKLIM
LPGEEIIHVL PQEYKVDGQG EIREPIGMYG GRLEANFHVV VGQVVSIKNV GRCIKSAGLD
LGNITLEPLA SSDAVLSQEE KEAGVALIDI GGGTTDLAIF KDGIIRHTAV IPFGGGVITE
DIKEGCSIIE KQAELLKTRF GSAWPGENRD NEIVSIPGLR GREPKEISLK NLSKIIHARV
VEIIEQVYVE IKNYGHEEQK KKLIAGIVLT GGGSQLKHLK QLVEYITGMD TRIGYPNEHL
AGDSDEEVAS PLYATAVGLL MNAIKNEKKL NSIKKKAQAS EGFVQAEQEE VEAFAGVEED
EFGSKNRMYK ERKSVFDKWS EKLKEFLDNA E
//
