ID A0A0D0RQD6_STAGA Unreviewed; 471 AA.
AC A0A0D0RQD6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 41.
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:RIL44524.1};
GN ORFNames=BUZ01_00705 {ECO:0000313|EMBL:RIL44524.1};
OS Staphylococcus gallinarum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1293 {ECO:0000313|EMBL:RIL44524.1, ECO:0000313|Proteomes:UP000283576};
RN [1] {ECO:0000313|EMBL:RIL44524.1, ECO:0000313|Proteomes:UP000283576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 1388 {ECO:0000313|EMBL:RIL44524.1,
RC ECO:0000313|Proteomes:UP000283576};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
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:RIL44524.1}.
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DR EMBL; QXRZ01000001; RIL44524.1; -; Genomic_DNA.
DR RefSeq; WP_042738929.1; NZ_RXWT01000100.1.
DR AlphaFoldDB; A0A0D0RQD6; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000283576; 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; -; 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|HAMAP-Rule:MF_02033,
KW ECO:0000256|PIRNR:PIRNR003101};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02033,
KW ECO:0000256|PIRNR:PIRNR003101};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02033}.
SQ SEQUENCE 471 AA; 52403 MW; 28B322D2018F88FE CRC64;
MEEHYYVSID IGSSSVKTIV GEKFHNGINV IGTGQTYTSG IKNGQIDDFD IAKQAVKDTI
KKASIASGVD IKEVFLKLPI VGTEVFDESN EIEFYEDTEL NGTHIEHVLE GIREKNNVPE
TEIINAFPIK FLVDGDNEVS DPKELIARHS LKVNAGVIAI QKSILINMIK CVESCGVDVL
DVYSDAYNYN SVLSATEKEL GACVIDIGED LTQLAFYERG ELVDADAIEM AGRDITEDIA
EGLNTSYETA EKIKHQYGHA FFDSASDQDV FTVDQVDSEE DAQFTQKDLA DIIEARVEDI
FFEVFDVLQE LQLTKVNGGF VVTGGSANLL GVKELLQDMV SEKVRIHTPS QMGIRKPEFS
SAISTISSSI TFDELLDYVT ISNHDSEEFE EEVIESDETT NNTKTSGFDW FKKKSNKQDE
APASDSSSED SQVTETYDEE VNADSDVEHK SQHNEQKDES KFKKLMKSLF D
//
