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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
 
 
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