RODZ_ECOLI
ID RODZ_ECOLI Reviewed; 337 AA.
AC P27434; P76987; P77137;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cytoskeleton protein RodZ;
GN Name=rodZ; Synonyms=yfgA; OrderedLocusNames=b2516, JW2500;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RC STRAIN=K12;
RX PubMed=7926684; DOI=10.1111/j.1574-6968.1994.tb07115.x;
RA Baker J., Parker J.;
RT "Sequence and characterization of the Escherichia coli genome between the
RT ndk and gcpE genes.";
RL FEMS Microbiol. Lett. 121:293-296(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 158-243.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-337.
RX PubMed=1521767; DOI=10.1016/0378-1097(92)90604-m;
RA Baker J., Franklin D.B., Parker J.;
RT "Sequence and characterization of the gcpE gene of Escherichia coli.";
RL FEMS Microbiol. Lett. 73:175-180(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-55.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7764507; DOI=10.1271/bbb.58.117;
RA Talukder A.A., Yanai S., Yamada M.;
RT "Analysis of products of the Escherichia coli genomic genes and regulation
RT of their expressions: an applicable procedure for genomic analysis of other
RT microorganisms.";
RL Biosci. Biotechnol. Biochem. 58:117-120(1994).
RN [8]
RP FUNCTION IN DETERMINATION OF CELL SHAPE, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19008860; DOI=10.1038/emboj.2008.234;
RA Shiomi D., Sakai M., Niki H.;
RT "Determination of bacterial rod shape by a novel cytoskeletal membrane
RT protein.";
RL EMBO J. 27:3081-3091(2008).
CC -!- FUNCTION: Cytoskeletal protein that is involved in cell-shape control
CC through regulation of the length of the long axis.
CC {ECO:0000269|PubMed:19008860}.
CC -!- INTERACTION:
CC P27434; P0A9X4: mreB; NbExp=3; IntAct=EBI-1129185, EBI-371008;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:19008860}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:19008860}. Note=Forms helical filaments along the
CC long axis of the cell.
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 -!- DISRUPTION PHENOTYPE: Affects the lengths of both the long and short
CC axes of the cell, but especially the long axis. Cells become shorter
CC and fatter and form round or oval shapes.
CC {ECO:0000269|PubMed:19008860}.
CC -!- SIMILARITY: Belongs to the RodZ family. {ECO:0000305}.
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DR EMBL; U00096; AAC75569.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16403.1; -; Genomic_DNA.
DR EMBL; U02965; AAA21360.1; -; Genomic_DNA.
DR EMBL; U83188; AAB40289.1; -; Genomic_DNA.
DR EMBL; X64451; CAA45782.1; -; Genomic_DNA.
DR EMBL; D21149; BAA04685.1; -; Genomic_DNA.
DR PIR; C65028; C65028.
DR RefSeq; NP_417011.1; NC_000913.3.
DR RefSeq; WP_001090866.1; NZ_LN832404.1.
DR AlphaFoldDB; P27434; -.
DR SMR; P27434; -.
DR BioGRID; 4261301; 535.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-12034N; -.
DR IntAct; P27434; 13.
DR MINT; P27434; -.
DR STRING; 511145.b2516; -.
DR jPOST; P27434; -.
DR PaxDb; P27434; -.
DR PRIDE; P27434; -.
DR EnsemblBacteria; AAC75569; AAC75569; b2516.
DR EnsemblBacteria; BAA16403; BAA16403; BAA16403.
DR GeneID; 946992; -.
DR KEGG; ecj:JW2500; -.
DR KEGG; eco:b2516; -.
DR PATRIC; fig|1411691.4.peg.4220; -.
DR EchoBASE; EB0015; -.
DR eggNOG; COG1426; Bacteria.
DR HOGENOM; CLU_047530_3_1_6; -.
DR InParanoid; P27434; -.
DR OMA; ADCWTQV; -.
DR PhylomeDB; P27434; -.
DR BioCyc; EcoCyc:EG10015-MON; -.
DR PRO; PR:P27434; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IC:ComplexPortal.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000149761"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..337
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..71
FT /note="HTH cro/C1-type"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 144..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 27
FT /note="G -> E (in Ref. 7; BAA04685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36192 MW; 67F90B10319F61C0 CRC64;
MNTEATHDQN EALTTGARLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPADLASTF
LRGYIRSYAR LVHIPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMTFTWLV
LFVVIGLSGA WWWQDRKAQQ EEITTMADQS SAELSSNSEQ GQSVPLNTST TTDPATTSTP
PASVDTTATN TQTPAVTAPA PAVDPQQNAV VSPSQANVDT AATPAPTAAT TPDGAAPLPT
DQAGVTTPVA DPNALVMNFT ADCWLEVTDA TGKKLFSGMQ RKDGNLNLTG QAPYKLKIGA
PAAVQIQYQG KPVDLSRFIR TNQVARLTLN AEQSPAQ
