ID A0A0F5JM17_9BACT Unreviewed; 447 AA.
AC A0A0F5JM17;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=HMPREF1536_01374 {ECO:0000313|EMBL:KKB58497.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB58497.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB58497.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB58497.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL Submitted (APR-2013) 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:KKB58497.1}.
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DR EMBL; AQHW01000009; KKB58497.1; -; Genomic_DNA.
DR RefSeq; WP_028727173.1; NZ_KQ033919.1.
DR AlphaFoldDB; A0A0F5JM17; -.
DR STRING; 1203610.HMPREF1536_01374; -.
DR PATRIC; fig|1203610.3.peg.1406; -.
DR HOGENOM; CLU_037850_4_0_10; -.
DR Proteomes; UP000033035; 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; 3.30.420.40; -; 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 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:UP000033035}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 397..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 48382 MW; FDFFFCE8391F5200 CRC64;
MAYTDFIAAI DLGSSHMVGM VGTKGPTGAL SIIAYEVENS ATCIRRGCVY NVEETANKIK
RLILKLENKL GGARIGKVYV GIGGQSLRSI DHTVPRILGT DGVVTEEIID GLYEECRNYH
PDMLDVLAAV SPTYFLDEKP EPNPVGIPCT RIEARYKLIV GRPSLKRYVL NSIGDRARIE
IADIVVSPLA LADVVLTDNE KDLGCALIGF GAGVTTLTVY KGGQLVNLSV IPFGGNLITR
DITSLHLVET EAERVKLTYG SAQMEKDNDL SIQVSSADGM GLREIKLADL NNVVEARMKE
ILENVYARLE ATGLMNSLGA GIVITGGGAA LKNLPEVIRE RLNMDVRYSA VRKGIVESGE
MIANNPEYAV AVGLLAKGTE NCALYIPPKV EVKVEKPVEE VKEEVKPTPE PPKKKPEKKK
GPGLFGRLTK GIDTFGKSLF DDEDDVK
//
