cell division protein ZipA [Salmonella sp. 32020114201800008SM]
Protein Classification
cell division protein ZipA; cell division protein ZipA C-terminal FtsZ-binding domain-containing protein; zipA and ZipA_C domain-containing protein( domain architecture ID 17594146)
cell division protein ZipA C-terminal FtsZ-binding domain-containing protein; cell division protein ZipA is an essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring; also required for the recruitment to the septal ring of downstream cell division proteins; zipA and ZipA_C domain-containing protein
cell division protein ZipA; This model represents the full length of bacterial cell division ...
21-320
4.43e-81
cell division protein ZipA; This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ. [Cellular processes, Cell division]
Pssm-ID: 274030 [Multi-domain] Cd Length: 284 Bit Score: 247.90 E-value: 4.43e-81
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential ...
192-320
1.31e-76
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential gene products necessary for assembly of the septal ring which mediates cell division in E.coli. ZipA and FtsA directly bind FtsZ, a homolog of eukaryotic tubulins, at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein.
Pssm-ID: 238142 Cd Length: 130 Bit Score: 230.72 E-value: 1.31e-76
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell ...
191-320
1.08e-64
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell division in E.coli. It interacts with the FtsZ protein in one of the initial steps of septum formation. The structure of this domain is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands.
Pssm-ID: 129010 Cd Length: 131 Bit Score: 200.19 E-value: 1.08e-64
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA ...
194-319
6.05e-59
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring. The structure of this domain is an alpha-beta fold with three alpha helices and a beta sheet of six antiparallel beta strands. The major loops protruding from the beta sheet surface are thought to form a binding site for FtsZ.
Pssm-ID: 427889 Cd Length: 127 Bit Score: 185.39 E-value: 6.05e-59
cell division protein ZipA; This model represents the full length of bacterial cell division ...
21-320
4.43e-81
cell division protein ZipA; This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ. [Cellular processes, Cell division]
Pssm-ID: 274030 [Multi-domain] Cd Length: 284 Bit Score: 247.90 E-value: 4.43e-81
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential ...
192-320
1.31e-76
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential gene products necessary for assembly of the septal ring which mediates cell division in E.coli. ZipA and FtsA directly bind FtsZ, a homolog of eukaryotic tubulins, at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein.
Pssm-ID: 238142 Cd Length: 130 Bit Score: 230.72 E-value: 1.31e-76
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell ...
191-320
1.08e-64
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell division in E.coli. It interacts with the FtsZ protein in one of the initial steps of septum formation. The structure of this domain is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands.
Pssm-ID: 129010 Cd Length: 131 Bit Score: 200.19 E-value: 1.08e-64
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA ...
194-319
6.05e-59
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring. The structure of this domain is an alpha-beta fold with three alpha helices and a beta sheet of six antiparallel beta strands. The major loops protruding from the beta sheet surface are thought to form a binding site for FtsZ.
Pssm-ID: 427889 Cd Length: 127 Bit Score: 185.39 E-value: 6.05e-59
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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