ID A0A119CVP9_THIDE Unreviewed; 100 AA.
AC A0A119CVP9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cell division protein ZapA {ECO:0000256|ARBA:ARBA00015195};
DE AltName: Full=Z ring-associated protein ZapA {ECO:0000256|ARBA:ARBA00033158};
GN ORFNames=ABW22_09705 {ECO:0000313|EMBL:KVW95448.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW95448.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW95448.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW95448.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
CC -!- FUNCTION: Activator of cell division through the inhibition of FtsZ
CC GTPase activity, therefore promoting FtsZ assembly into bundles of
CC protofilaments necessary for the formation of the division Z ring. It
CC is recruited early at mid-cell but it is not essential for cell
CC division. {ECO:0000256|ARBA:ARBA00024910}.
CC -!- SUBUNIT: Homodimer. Interacts with FtsZ.
CC {ECO:0000256|ARBA:ARBA00026068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KVW95448.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDUG01000025; KVW95448.1; -; Genomic_DNA.
DR RefSeq; WP_059755562.1; NZ_LDUG01000025.1.
DR AlphaFoldDB; A0A119CVP9; -.
DR STRING; 1123392.GCA_000376425_02153; -.
DR PATRIC; fig|36861.3.peg.1600; -.
DR OrthoDB; 5297208at2; -.
DR Proteomes; UP000064243; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.50; -; 1.
DR Gene3D; 3.30.160.880; Cell division protein ZapA protomer, N-terminal domain; 1.
DR InterPro; IPR007838; Cell_div_ZapA-like.
DR InterPro; IPR036192; Cell_div_ZapA-like_sf.
DR InterPro; IPR042233; Cell_div_ZapA_N.
DR PANTHER; PTHR34981; CELL DIVISION PROTEIN ZAPA; 1.
DR PANTHER; PTHR34981:SF1; CELL DIVISION PROTEIN ZAPA; 1.
DR Pfam; PF05164; ZapA; 1.
DR SUPFAM; SSF102829; Cell division protein ZapA-like; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:KVW95448.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
SQ SEQUENCE 100 AA; 11010 MW; C91D49475EFEBD88 CRC64;
MAGPRSIEIH ILGRAYKVAC SREEESALIA AADYLDEKMR EIRESSKVIG AERIAIMAGL
NLAHELLTQG GGGRTEETRA RLTHCNALLD TVLEDQDKLF
//
