ID   RODZ_YERPS              Reviewed;         362 AA.
AC   Q667Z8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN   Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=YPTB2842;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH22080.1; -; Genomic_DNA.
DR   RefSeq; WP_011192802.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q667Z8; -.
DR   SMR; Q667Z8; -.
DR   EnsemblBacteria; CAH22080; CAH22080; YPTB2842.
DR   GeneID; 66844735; -.
DR   KEGG; ypo:BZ17_3788; -.
DR   KEGG; yps:YPTB2842; -.
DR   PATRIC; fig|273123.14.peg.3974; -.
DR   OMA; ADCWTQV; -.
DR   Proteomes; UP000001011; 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..362
FT                   /note="Cytoskeleton protein RodZ"
FT                   /id="PRO_0000361874"
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..362
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT   DOMAIN          19..79
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          151..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  38058 MW;  080326AD0BB1FD8B CRC64;
     MNTEASQDQT VTETPGVRLR QARESLGLTQ QTVAERLCLK VSTIRDIEED NAQANLASTF
     HRGYIRSYAK LVHLPEDELL PILEKQAPVR AAKVAPMQSF SLGKKHKKRD GWLMSFTWLI
     VLVVLGLTGA WWWQNHQAQQ AEIANMVDQS SAQLSQNGGQ PVPLTDDNSD AIAPTDAPAP
     VANGQPVPLT NHSTSAVTNS ATTSSATTSS VPTTSSVPKT TLVPKTNSTE PVDTANTNTT
     MHQEGAASAA VSPSQVPQPG LSTGPSPLPT ADAGVSGSTS SVGALVMNFT ADCWLQVVDA
     TGKTLFSGIQ KGGAVLNLAG KAPYKLTIGA PGALTISYQG NPVDLSKFIK ANRVARLTVG
     VE