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ZIPA_ECO5E
ID   ZIPA_ECO5E              Reviewed;         332 AA.
AC   B5YZV9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   OrderedLocusNames=ECH74115_3643;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI39065.1; -; Genomic_DNA.
DR   RefSeq; WP_001299866.1; NC_011353.1.
DR   AlphaFoldDB; B5YZV9; -.
DR   SMR; B5YZV9; -.
DR   PRIDE; B5YZV9; -.
DR   KEGG; ecf:ECH74115_3643; -.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   OMA; FWSIRKQ; -.
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..332
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_1000127216"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   TOPO_DOM        28..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   REGION          42..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  36947 MW;  6718C9C75C5476D2 CRC64;
     MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD
     EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ PRQPVQQPPE AQVPPQHAPR
     PAQPVQQPVQ QPAYQPQPEQ PLQQPVSPQV APAPQPVHSA PQPAQQAFQP AEPVAAPQPE
     PVAEPAPVMD KPKRKEAVII MNVAAHHGSE LNGELLLNSI QQAGFIFGDM NIYHRHLSPD
     GSGPALFSLA NMVKPGTFDP EMKDFTTPGV TIFMQVPSYG DELQNFKLML QSAQHIADEV
     GGVVLDDQRR MMTPQKLREY QDIIREVKDA NA
 
 
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