ID   RODZ_SALSV              Reviewed;         334 AA.
AC   B4TR96;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN   Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=SeSA_A2763;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF92274.1; -; Genomic_DNA.
DR   RefSeq; WP_001090883.1; NC_011094.1.
DR   AlphaFoldDB; B4TR96; -.
DR   SMR; B4TR96; -.
DR   EnsemblBacteria; ACF92274; ACF92274; SeSA_A2763.
DR   KEGG; sew:SeSA_A2763; -.
DR   HOGENOM; CLU_047530_3_1_6; -.
DR   OMA; ADCWTQV; -.
DR   Proteomes; UP000001865; 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..334
FT                   /note="Cytoskeleton protein RodZ"
FT                   /id="PRO_0000361858"
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..334
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..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  35833 MW;  5E9BA5BEB79CAF81 CRC64;
     MNTEATHDQN EAQTTGVRLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPSDLASTF
     LRGYIRSYAR LVHVPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMSFTWLV
     LFVVVGLTGA WWWQNHKAQQ EEITTMADQS TAELNADKDS GQNVPLDTRD ATSQDTTPAQ
     TAPAPATPVD STAATQTPAA TATATQNTVV APSQANVDTA ATSAAPAATE TPSALPTSQA
     GVAAPAADPN ALVMNFTADC WLEVTDATGK KLFSGMQRKD GNLNLTGQAP YKLKIGAPAA
     VQIQYQGKPV DLSRFIRTNQ VARLTLNAEP TPAQ