ID T0CG95_ALIAG Unreviewed; 409 AA.
AC T0CG95; A0A9E6ZU95;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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:UNO50585.1};
GN ORFNames=K1I37_09135 {ECO:0000313|EMBL:UNO50585.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO50585.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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}.
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DR EMBL; CP080467; UNO50585.1; -; Genomic_DNA.
DR RefSeq; WP_021295403.1; NZ_AURB01000068.1.
DR STRING; 1356854.N007_02870; -.
DR KEGG; aaco:K1I37_09135; -.
DR Proteomes; UP000829401; 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000829401}.
SQ SEQUENCE 409 AA; 43747 MW; 99A80FE5F8CF0BDD CRC64;
MAKEDYIVSL DIGTSKIRAI IGEPTGSSIN VIGVGSASGE GLRHGSIVDI DLTVESIREA
IDHAERMVGI HISSAYVGIS GNHIQLHSSH GVVAVSSADR EISDEDIERV LQQARVVALP
PEREVIDVVA KEFVVDGLRG IMDPRGMLGV RLEVEAYLIT GSRTAIHNVV RCVERAGLEV
ANLVLMPLAA SHIALSNDER KLGVALVDIG AGATTVTIFS NGVLMGTSII PMGGDYVTHD
IAIGLRTSTT SAEQVKLRHA CAVVAQASEN ETFQVPRMGS NKDTEYTQYD LATIVEPRMQ
EIFALVQKEV EKMGYADDLP AGYVLHGGVM STPGAAELAS EELQAPVRIA IPEFLGVRDP
SFVNGVGTIA YAARTGLRPT PMDQSAPVRQ VKSSGGMFTR IKDWLRDFV
//
