ID J6IAK2_9FLAO Unreviewed; 473 AA.
AC J6IAK2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ECO:0000313|EMBL:EJU29768.1};
GN ORFNames=HMPREF1154_0362 {ECO:0000313|EMBL:EJU29768.1};
OS Capnocytophaga sp. CM59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=936370 {ECO:0000313|EMBL:EJU29768.1, ECO:0000313|Proteomes:UP000003140};
RN [1] {ECO:0000313|EMBL:EJU29768.1, ECO:0000313|Proteomes:UP000003140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM59 {ECO:0000313|EMBL:EJU29768.1,
RC ECO:0000313|Proteomes:UP000003140};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU29768.1}.
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DR EMBL; ALNN01000031; EJU29768.1; -; Genomic_DNA.
DR AlphaFoldDB; J6IAK2; -.
DR PATRIC; fig|936370.3.peg.1571; -.
DR Proteomes; UP000003140; 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; -; 1.
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 13..202
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 398..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52290 MW; 2233CA982D3B63E4 CRC64;
MKTENKMNQR KYFAGIDIGT TKIVAIIGCE NQYGKLEILG YGKAKSQGIF RGMVGNIGKT
IDSIEQAVAQ AQAKAGVIIS EAYVGIAGQH IKSNEASDYI TRENAEEIIT VKDLEALCQC
VMSSKNRYPG EEVIHILPQE YKVDNQEDIH DPIGMVGSRL EGTFHIVTGQ VAPIKNIQRC
VTKAGIALKG LTLEPIASSA SVLSEEEKEA GVALVDIGGG TTDLAIFKEG YIRYTAVVPF
GGNIIDKDIR EGCNVFDKQA EQLKIRFGSA WPEYTKENEV INIQMFKGRE PQEIQVTNLA
RIIRCRMEEI IEAIFNEIKN YGYDQPRKKL IAGIVLTGGG SELKDLPQLV EYLTGLPTRI
GHPNEHLASN TPTELSSPIY ATAIGLLLDG IEREHSEGQR IDFSQLSETP TQEPTATIEP
EEEAPAVAEP VVLPVAEQEP EKEKEKEEEH KPEKKNIIRT LSDKFTDFFK TME
//
