RODZ_SERP5
ID RODZ_SERP5 Reviewed; 323 AA.
AC A8GHW6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=Spro_3610;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-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; CP000826; ABV42706.1; -; Genomic_DNA.
DR RefSeq; WP_012146318.1; NC_009832.1.
DR AlphaFoldDB; A8GHW6; -.
DR SMR; A8GHW6; -.
DR STRING; 399741.Spro_3610; -.
DR PRIDE; A8GHW6; -.
DR EnsemblBacteria; ABV42706; ABV42706; Spro_3610.
DR KEGG; spe:Spro_3610; -.
DR eggNOG; COG1426; Bacteria.
DR HOGENOM; CLU_047530_3_1_6; -.
DR OMA; ADCWTQV; -.
DR OrthoDB; 2071222at2; -.
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..323
FT /note="Cytoskeleton protein RodZ"
FT /id="PRO_0000361861"
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..323
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 149..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 34499 MW; EEAEBF75484C466A CRC64;
MNTEASQDKT VSMTTGERLR QAREQLGLSQ QAVAERLCLK MSTVRDIEED NLSADLASTF
VRGYIRSYAK LVRLPEDELL PMLAKQAPLK VAKVAPMQSF SLGKRRKKRD GWLMSFTWLI
VFVVVGLTGA WWWQNHKAQQ EEIVTMADQS SAQLSQNNEG QSVPLTDSNA DNSAPLADNG
STPVDTGVAP QQSQTPAVSG SATAQQPAVV SPSQTTLPET TPAAPTAPLP TADAGVTAPA
VDPNALVMEF SADCWLQVSD ANGKTLYSGS QKSGGKLSLA GTAPYKLTIG APAAVQIQYQ
GKPVDLSRFV KSNRVARLTV AAQ