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ZIPA_SALTY
ID   ZIPA_SALTY              Reviewed;         328 AA.
AC   P0A2N6; P55894;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; OrderedLocusNames=STM2428;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC   STRAIN=LT2;
RX   PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA   Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT   "DNA sequences of the cysK regions of Salmonella typhimurium and
RT   Escherichia coli and linkage of the cysK regions to ptsH.";
RL   J. Bacteriol. 170:3150-3157(1988).
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; AE006468; AAL21322.1; -; Genomic_DNA.
DR   EMBL; M21450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_461363.1; NC_003197.2.
DR   RefSeq; WP_000983126.1; NC_003197.2.
DR   AlphaFoldDB; P0A2N6; -.
DR   SMR; P0A2N6; -.
DR   STRING; 99287.STM2428; -.
DR   PaxDb; P0A2N6; -.
DR   EnsemblBacteria; AAL21322; AAL21322; STM2428.
DR   GeneID; 1253950; -.
DR   KEGG; stm:STM2428; -.
DR   PATRIC; fig|99287.12.peg.2565; -.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   OMA; FWSIRKQ; -.
DR   PhylomeDB; P0A2N6; -.
DR   BioCyc; SENT99287:STM2428-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_0000214535"
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..328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT   REGION          42..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..166
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  36318 MW;  B8A44F708AF35F13 CRC64;
     MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDDDVEED
     EGVGEVRVHR VNHAPGQSQE HDAPRQSPQH QYQPPYASAQ PRPAAPPQPQ APMQQPVQQP
     VQPAPQPQQV QPSAPPVQPP QQQPAPPSQA PQPVAQPAPP PSAQTFQPAE PVVEAEPVVE
     EAPVVEKPQR KEAVIIMNVA AHHGSELNGE VLLNSIQQSG FKFGDMNIFH RHLSPDGSGP
     ALFSLANMVN PGTFDPEMTD FTTPGVTIFM QVPSYGDALQ NFKLMLQSAQ HIADEVGGVV
     LDDQRRMMTP QKLREYQDRI REVMDANA
 
 
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