ID   RODZ_ECOL5              Reviewed;         335 AA.
AC   Q0TEW9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN   Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=ECP_2521;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG70510.1; -; Genomic_DNA.
DR   RefSeq; WP_001090872.1; NC_008253.1.
DR   AlphaFoldDB; Q0TEW9; -.
DR   SMR; Q0TEW9; -.
DR   STRING; 362663.ECP_2521; -.
DR   EnsemblBacteria; ABG70510; ABG70510; ECP_2521.
DR   KEGG; ecp:ECP_2521; -.
DR   HOGENOM; CLU_047530_3_1_6; -.
DR   OMA; ADCWTQV; -.
DR   Proteomes; UP000009182; 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..335
FT                   /note="Cytoskeleton protein RodZ"
FT                   /id="PRO_0000361843"
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..335
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          148..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  36142 MW;  0F78E62CE69E1CA5 CRC64;
     MNTEATHDQN EALTTGARLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPADLASTF
     LRGYIRSYAR LVHIPEEELQ PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMTFTWLV
     LFVVIGLSGA WWWQDHKAQQ EEITTMADQS SAELNNNQSQ SVPLDTSTTT DQAMATTPTS
     PVDTTATNTQ TPAVTAPAPA VDPQQNAVVP PSQANVDTAA TPAPAATTTP DGAAPLPTDQ
     AGVTTPAVDP NALVMNFTAD CWLEVTDATG KKLFSGMQRK DGNLNLTGQA PYKLKIGAPA
     AVQIQYQGKP VDLSRFIRTN QVARLTLNAE QSPAQ