ZIPA_PSEA8
ID ZIPA_PSEA8 Reviewed; 289 AA.
AC B7UVJ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=PLES_38001;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
CC -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ
CC protofilaments by cross-linking them and that serves as a cytoplasmic
CC membrane anchor for the Z ring. Also required for the recruitment to
CC the septal ring of downstream cell division proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SUBUNIT: Interacts with FtsZ via their C-terminal domains.
CC {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00509}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00509}. Note=Localizes to the Z ring in an FtsZ-dependent
CC manner. {ECO:0000255|HAMAP-Rule:MF_00509}.
CC -!- SIMILARITY: Belongs to the ZipA family. {ECO:0000255|HAMAP-
CC Rule:MF_00509}.
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DR EMBL; FM209186; CAW28527.1; -; Genomic_DNA.
DR RefSeq; WP_003083352.1; NC_011770.1.
DR AlphaFoldDB; B7UVJ4; -.
DR SMR; B7UVJ4; -.
DR KEGG; pag:PLES_38001; -.
DR HOGENOM; CLU_030174_0_1_6; -.
DR OMA; LDTHKEP; -.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0090529; P:cell septum assembly; IEA:InterPro.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR CDD; cd00231; ZipA; 1.
DR Gene3D; 3.30.1400.10; -; 1.
DR HAMAP; MF_00509; ZipA; 1.
DR InterPro; IPR011919; Cell_div_ZipA.
DR InterPro; IPR007449; ZipA_FtsZ-bd_C.
DR InterPro; IPR036765; ZipA_FtsZ-bd_C_sf.
DR PANTHER; PTHR38685; PTHR38685; 1.
DR Pfam; PF04354; ZipA_C; 1.
DR SMART; SM00771; ZipA_C; 1.
DR SUPFAM; SSF64383; SSF64383; 1.
DR TIGRFAMs; TIGR02205; septum_zipA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Cell division protein ZipA"
FT /id="PRO_1000127222"
FT TOPO_DOM 1
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TOPO_DOM 23..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT REGION 66..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32237 MW; 720D6FED832B329C CRC64;
MDIGLREWLI VIGLIVIAGI LFDGWRRMRG GKGKLKFKLD RSFANLPDDD GDSAELLGPA
RVVEHREPSF DEQDLPSVSA REAKERKGGK RQEEPRQGDL DLDEGLALEA DPSDAAETVE
PRKGKSKGRK EKEREKAPAV AAEPAPVDEV LIINVIARDE SGFKGPALLQ NILESGLRFG
DMDIFHRHES MAGNGEILFS MANAVKPGTF DLDDIDNFST RAVSFFLGLP GPRHPKQAFD
VMVAAARKLA HELNGELKDE QRSVLTAQTI EHYRQRIIDH ERRSLMQKR