ID   RODZ_SALAR              Reviewed;         321 AA.
AC   A9MHL4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN   Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=SARI_00354;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX20292.1; -; Genomic_DNA.
DR   RefSeq; WP_001090878.1; NC_010067.1.
DR   AlphaFoldDB; A9MHL4; -.
DR   SMR; A9MHL4; -.
DR   STRING; 41514.SARI_00354; -.
DR   EnsemblBacteria; ABX20292; ABX20292; SARI_00354.
DR   KEGG; ses:SARI_00354; -.
DR   HOGENOM; CLU_047530_3_1_6; -.
DR   OMA; ADCWTQV; -.
DR   OrthoDB; 2071222at2; -.
DR   Proteomes; UP000002084; 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   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..321
FT                   /note="Cytoskeleton protein RodZ"
FT                   /id="PRO_0000361848"
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..321
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          167..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   321 AA;  34580 MW;  1546F5585315C3B6 CRC64;
     MNTEATHDQN EAQTTGVRLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPSDLASTF
     LRGYIRSYAR LVHVPEEELL PGLEKQAPLR AAKVAPMQNF SLGKRRKKRD GWLMSFTWLV
     LFVVVGLTGA WWWQNHKAQQ EEITTMADQS TAELNADKDS GQGVQLDTRA AASQDTTPAE
     TAPAAPVDST AAATQNTVVA PSQANVDTAA TSATATETSS ALPTDQAGVA APAADSNALV
     MNFTADCWLE VTDATGKKLF SGMQRKDGNL NLTGQAPYKL KIGAPAAVQI QYQGKPVDLS
     RFIRTNQVAR LTINAEPTSA Q