RODZ_SALTI
ID RODZ_SALTI Reviewed; 324 AA.
AC Q8Z4P3; Q7CBJ9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN OrderedLocusNames=STY2769, t0332;
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: Cytoskeletal protein that is involved in cell-shape control
CC through regulation of the length of the long axis. {ECO:0000255|HAMAP-
CC Rule:MF_02017}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02017}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02017}. Note=Forms helical filaments along
CC the long axis of the cell. {ECO:0000255|HAMAP-Rule:MF_02017}.
CC -!- DOMAIN: The helix-turn-helix (HTH) motif in the cytoplasmic domain of
CC the N-terminus is involved in the formation of spirals to maintain the
CC rigid rod shape. As this protein is anchored in the cytoplasmic
CC membrane, the HTH motif may contribute to protein-protein interactions
CC to form the RodZ helix, which is localized beneath the cytoplasmic
CC membrane. The C-terminal domain may be critical for determination of
CC the rod shape by probably interacting with enzymes required for
CC synthesis of the peptidoglycan layer, including PBPs in the periplasm.
CC {ECO:0000255|HAMAP-Rule:MF_02017}.
CC -!- SIMILARITY: Belongs to the RodZ family. {ECO:0000255|HAMAP-
CC Rule:MF_02017}.
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DR EMBL; AE014613; AAO68055.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02727.1; -; Genomic_DNA.
DR RefSeq; NP_457056.1; NC_003198.1.
DR RefSeq; WP_001090905.1; NZ_WSUR01000007.1.
DR AlphaFoldDB; Q8Z4P3; -.
DR SMR; Q8Z4P3; -.
DR STRING; 220341.16503739; -.
DR EnsemblBacteria; AAO68055; AAO68055; t0332.
DR KEGG; stt:t0332; -.
DR KEGG; sty:STY2769; -.
DR PATRIC; fig|220341.7.peg.2811; -.
DR eggNOG; COG1426; Bacteria.
DR HOGENOM; CLU_047530_3_1_6; -.
DR OMA; ADCWTQV; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR HAMAP; MF_02017; RodZ; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR025194; DUF4115.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR023690; RodZ.
DR Pfam; PF13464; DUF4115; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape; DNA-binding; Membrane;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..324
FT /note="Cytoskeleton protein RodZ"
FT /id="PRO_0000361859"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT TRANSMEM 112..132
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT TOPO_DOM 133..324
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT DOMAIN 19..71
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT REGION 155..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 34779 MW; D0E2CA01B2678F93 CRC64;
MNTEATHDQN EAQTTGVRLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPSDLASTF
LRGYIRSYAR LVHVPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMSFTWLV
LFVVVGLTGA WWWQNHKAQQ EEITTMADQS TAELNADKDS GQSVPLDTSA ATSQDTTPAQ
TAPAPATPVD STAATQNTVV APSQANVDTA ATSAAPAATE TPSALPTSQA GVAAPAADPN
ALVMNFTADC WLEVTDATGK KLFSGMQRKD GNLNLTGQAP YKLKIGAPAA VQIQYQGKPV
DLSRFIRTNQ VARLTLNAEP TPAQ
