FTSA_STAAW
ID FTSA_STAAW Reviewed; 470 AA.
AC Q8NX33;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; OrderedLocusNames=MW1068;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC Rule:MF_02033}.
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}.
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DR EMBL; BA000033; BAB94933.1; -; Genomic_DNA.
DR RefSeq; WP_000391033.1; NC_003923.1.
DR PDB; 3WT0; X-ray; 2.00 A; A/B/C/D=1-384.
DR PDBsum; 3WT0; -.
DR AlphaFoldDB; Q8NX33; -.
DR SMR; Q8NX33; -.
DR EnsemblBacteria; BAB94933; BAB94933; BAB94933.
DR KEGG; sam:MW1068; -.
DR HOGENOM; CLU_037850_1_0_9; -.
DR OMA; DGIIRHT; -.
DR Proteomes; UP000000418; Chromosome.
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 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 3D-structure; Cell cycle; Cell division; Cell membrane; Membrane.
FT CHAIN 1..470
FT /note="Cell division protein FtsA"
FT /id="PRO_0000062752"
FT REGION 416..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 13..24
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 80..93
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 121..133
FT /evidence="ECO:0007829|PDB:3WT0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 146..161
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:3WT0"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 286..311
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:3WT0"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3WT0"
FT HELIX 360..375
FT /evidence="ECO:0007829|PDB:3WT0"
SQ SEQUENCE 470 AA; 52908 MW; E3C26901FD2489FA 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 INYHDSEETE EDVIDVKDKD NESKLGGFDW FKRKTNKKDT
HENEVESTDE EIYQSEDNHQ EHKQNHEHVQ DKDKDKEESK FKKLMKSLFE
