RODZ_ENT38
ID RODZ_ENT38 Reviewed; 336 AA.
AC A4WD94;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=Ent638_3010;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP61674.1; -; Genomic_DNA.
DR RefSeq; WP_015960006.1; NC_009436.1.
DR AlphaFoldDB; A4WD94; -.
DR SMR; A4WD94; -.
DR STRING; 399742.Ent638_3010; -.
DR EnsemblBacteria; ABP61674; ABP61674; Ent638_3010.
DR KEGG; ent:Ent638_3010; -.
DR eggNOG; COG1426; Bacteria.
DR HOGENOM; CLU_047530_3_1_6; -.
DR OMA; ADCWTQV; -.
DR OrthoDB; 2071222at2; -.
DR Proteomes; UP000000230; 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..336
FT /note="Cytoskeleton protein RodZ"
FT /id="PRO_0000361831"
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..336
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 152..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36189 MW; 8C26EFEFFD9C2EAA CRC64;
MNTEATHDKT EALSTGVRLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPADLASTF
LRGYIRSYAK LVHIPEEELL PMMEKHAPVR AAKVAPMQTF SLGKRRKKRD GWLMSFTWLV
LFVVIGLTGA WWWQNHKAQQ EEITTMADQS SAALNNSGNN GAQSVPLNTD SASTSSEPQT
AETDSQTVEP VQTPAPAMTP DQTAAQNAVV SPSQANVDSA PAVTPTTTGN VNVTQPLPTD
QAGVAATTAD ANALVMNFSA DCWLEVTDAT GKKLFSGLQR KDGTLNLTGQ APYKLKIGAP
SAVQIQYQGK PVDLSRFIRT NQVARLTVSA EQSAAQ