RODZ_SHIFL
ID RODZ_SHIFL Reviewed; 337 AA.
AC Q83QK7; Q7C0G9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN OrderedLocusNames=SF2562, S2734;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN44062.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17889.1; -; Genomic_DNA.
DR RefSeq; NP_708355.1; NC_004337.2.
DR RefSeq; WP_001090857.1; NZ_WPGW01000078.1.
DR AlphaFoldDB; Q83QK7; -.
DR SMR; Q83QK7; -.
DR STRING; 198214.SF2562; -.
DR EnsemblBacteria; AAN44062; AAN44062; SF2562.
DR EnsemblBacteria; AAP17889; AAP17889; S2734.
DR GeneID; 1024372; -.
DR GeneID; 58390841; -.
DR KEGG; sfl:SF2562; -.
DR KEGG; sfx:S2734; -.
DR PATRIC; fig|198214.7.peg.3060; -.
DR HOGENOM; CLU_047530_3_1_6; -.
DR OMA; ADCWTQV; -.
DR OrthoDB; 2071222at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..337
FT /note="Cytoskeleton protein RodZ"
FT /id="PRO_0000361865"
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..337
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 145..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 36173 MW; 0F6CC292D8E426C0 CRC64;
MNTEATHDQN EALTTGARLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPADLASTF
LRGYIRSYAR LVHIPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMTFTWLV
LFVVIGLSGA WWWQDHKAQQ EEITTMADQS SAELSSNSEQ GQSVPLNTST TTDPATTSTP
PASVDTTATN TQTPAVTAPA PAVDPQQNAV VSPSQANVDT AATPVPTAAT TPDGAAPLPT
DQAGVTTPAA DPNALVMNFT ADCWLEVTDA TGKKLFSGMQ RKDGNLNLTG QAPYKLKIGA
PAAVQIQYQG KPVDLSRFIR TNQVARLTLN AEQSPAQ
