FTSA_STAA8
ID FTSA_STAA8 Reviewed; 470 AA.
AC O07325; Q2FZ90;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN OrderedLocusNames=SAOUHSC_01149;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9287029; DOI=10.1128/jb.179.17.5632-5635.1997;
RA Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RT "Identification and characterization of cell wall-cell division gene
RT clusters in pathogenic Gram-positive cocci.";
RL J. Bacteriol. 179:5632-5635(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP INTERACTION WITH FTSZ.
RC STRAIN=WCUH29 / NCIMB 40771;
RX PubMed=10753635; DOI=10.1006/bbrc.2000.2439;
RA Yan K., Pearce K.H., Payne D.J.;
RT "A conserved residue at the extreme C-terminus of FtsZ is critical for the
RT FtsA-FtsZ interaction in Staphylococcus aureus.";
RL Biochem. Biophys. Res. Commun. 270:387-392(2000).
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:0000255|HAMAP-Rule:MF_02033}.
CC -!- SUBUNIT: Self-interacts (By similarity). Interacts with FtsZ
CC (PubMed:10753635). {ECO:0000255|HAMAP-Rule:MF_02033,
CC ECO:0000269|PubMed:10753635}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02033};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02033};
CC Cytoplasmic side {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_02033}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02033}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45628.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U94706; AAC45628.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000253; ABD30259.1; -; Genomic_DNA.
DR RefSeq; WP_000391031.1; NZ_LS483365.1.
DR RefSeq; YP_499691.1; NC_007795.1.
DR AlphaFoldDB; O07325; -.
DR SMR; O07325; -.
DR STRING; 1280.SAXN108_1183; -.
DR EnsemblBacteria; ABD30259; ABD30259; SAOUHSC_01149.
DR GeneID; 3920709; -.
DR KEGG; sao:SAOUHSC_01149; -.
DR PATRIC; fig|93061.5.peg.1054; -.
DR eggNOG; COG0849; Bacteria.
DR HOGENOM; CLU_037850_1_0_9; -.
DR OMA; DGIIRHT; -.
DR PRO; PR:O07325; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR003494; SHS2_FtsA.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01174; ftsA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome.
FT CHAIN 1..470
FT /note="Cell division protein FtsA"
FT /id="PRO_0000062751"
FT REGION 416..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 52935 MW; 5EDEA401E8EB63DF CRC64;
MEEHYYVSID IGSSSVKTIV GEKFHNGINV IGTGQTYTSG IKNGLIDDFD IARQAIKDTI
KKASIASGVD IKEVFLKLPI IGTEVYDESN EIDFYEDTEI NGSHIEKVLE GIREKNDVQE
TEVINVFPIR FIVDKENEVS DPKELIARHS LKVEAGVIAI QKSILINMIK CVEACGVDVL
DVYSDAYNYG SILTATEKEL GACVIDIGED VTQVAFYERG ELVDADSIEM AGRDITDDIA
QGLNTSYETA EKVKHQYGHA FYDSASDQDI FTVEQVDSDE TVQYTQKDLS DFIEARVEEI
FFEVFDVLQD LGLTKVNGGF IVTGGSANLL GVKELLSDMV SEKVRIHTPS QMGIRKPEFS
SAISTISSSI AFDELLDYVT INYHDNEETE EDVIDVKDKD NESKLGGFDW FKRKTNKKDT
HENEVESTDE EIYQSEDNHQ EHKQNHEHVQ DKDKDKEESK FKKLMKSLFE