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ZIPA_SALTI
ID   ZIPA_SALTI              Reviewed;         328 AA.
AC   P0A2N7; P55894;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509};
GN   OrderedLocusNames=STY2664, t0429;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07660.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68147.1; -; Genomic_DNA.
DR   RefSeq; NP_456965.1; NC_003198.1.
DR   RefSeq; WP_000983126.1; NZ_WSUR01000025.1.
DR   AlphaFoldDB; P0A2N7; -.
DR   SMR; P0A2N7; -.
DR   STRING; 220341.16503647; -.
DR   EnsemblBacteria; AAO68147; AAO68147; t0429.
DR   KEGG; stt:t0429; -.
DR   KEGG; sty:STY2664; -.
DR   PATRIC; fig|220341.7.peg.2700; -.
DR   eggNOG; COG3115; Bacteria.
DR   HOGENOM; CLU_030174_1_0_6; -.
DR   OMA; FWSIRKQ; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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..328
FT                   /note="Cell division protein ZipA"
FT                   /id="PRO_0000214534"
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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