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Protein

Cytoskeleton protein RodZ

Gene

rodZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi30 – 4920H-T-H motifBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • regulation of cell shape Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell shape

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10015-MONOMER.
ECOL316407:JW2500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoskeleton protein RodZ
Gene namesi
Name:rodZ
Synonyms:yfgA
Ordered Locus Names:b2516, JW2500
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10015. yfgA.

Subcellular locationi

  • Cell inner membrane 1 Publication; Single-pass type II membrane protein 1 Publication

  • Note: Forms helical filaments along the long axis of the cell.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 111111CytoplasmicSequence analysisAdd
BLAST
Transmembranei112 – 13221Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini133 – 337205PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • Gram-negative-bacterium-type cell wall Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Affects the lengths of both the long and short axes of the cell, but especially the long axis. Cells become shorter and fatter and form round or oval shapes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Cytoskeleton protein RodZPRO_0000149761Add
BLAST

Proteomic databases

EPDiP27434.
PaxDbiP27434.
PRIDEiP27434.

Interactioni

Protein-protein interaction databases

BioGridi4261301. 515 interactions.
DIPiDIP-12034N.
IntActiP27434. 11 interactions.
MINTiMINT-7012109.
STRINGi511145.b2516.

Structurei

3D structure databases

ProteinModelPortaliP27434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 7153HTH cro/C1-typeAdd
BLAST

Domaini

The helix-turn-helix (HTH) motif in the cytoplasmic domain of the N-terminus is involved in the formation of spirals to maintain the rigid rod shape. As this protein is anchored in the cytoplasmic membrane, the HTH motif may contribute to protein-protein interactions to form the RodZ helix, which is localized beneath the cytoplasmic membrane. The C-terminal domain may be critical for determination of the rod shape by probably interacting with enzymes required for synthesis of the peptidoglycan layer, including PBPs in the periplasm.

Sequence similaritiesi

Belongs to the RodZ family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105HSZ. Bacteria.
COG1426. LUCA.
HOGENOMiHOG000276142.
InParanoidiP27434.
KOiK15539.
OMAiKLPGHTF.
OrthoDBiEOG65XN0H.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
HAMAPiMF_02017. RodZ.
InterProiIPR001387. Cro/C1-type_HTH.
IPR025194. DUF4115.
IPR010982. Lambda_DNA-bd_dom.
IPR023690. RodZ.
[Graphical view]
PfamiPF13464. DUF4115. 1 hit.
PF13413. HTH_25. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTEATHDQN EALTTGARLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED
60 70 80 90 100
KAPADLASTF LRGYIRSYAR LVHIPEEELL PGLEKQAPLR AAKVAPMQSF
110 120 130 140 150
SLGKRRKKRD GWLMTFTWLV LFVVIGLSGA WWWQDRKAQQ EEITTMADQS
160 170 180 190 200
SAELSSNSEQ GQSVPLNTST TTDPATTSTP PASVDTTATN TQTPAVTAPA
210 220 230 240 250
PAVDPQQNAV VSPSQANVDT AATPAPTAAT TPDGAAPLPT DQAGVTTPVA
260 270 280 290 300
DPNALVMNFT ADCWLEVTDA TGKKLFSGMQ RKDGNLNLTG QAPYKLKIGA
310 320 330
PAAVQIQYQG KPVDLSRFIR TNQVARLTLN AEQSPAQ
Length:337
Mass (Da):36,192
Last modified:June 1, 1994 - v2
Checksum:i67F90B10319F61C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271G → E in BAA04685 (PubMed:7764507).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75569.1.
AP009048 Genomic DNA. Translation: BAA16403.1.
U02965 Genomic DNA. Translation: AAA21360.1.
U83188 Genomic DNA. Translation: AAB40289.1.
X64451 Genomic DNA. Translation: CAA45782.1.
D21149 Genomic DNA. Translation: BAA04685.1.
PIRiC65028.
RefSeqiNP_417011.1. NC_000913.3.
WP_001090866.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75569; AAC75569; b2516.
BAA16403; BAA16403; BAA16403.
GeneIDi946992.
KEGGiecj:JW2500.
eco:b2516.
PATRICi32120425. VBIEscCol129921_2615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75569.1.
AP009048 Genomic DNA. Translation: BAA16403.1.
U02965 Genomic DNA. Translation: AAA21360.1.
U83188 Genomic DNA. Translation: AAB40289.1.
X64451 Genomic DNA. Translation: CAA45782.1.
D21149 Genomic DNA. Translation: BAA04685.1.
PIRiC65028.
RefSeqiNP_417011.1. NC_000913.3.
WP_001090866.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP27434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261301. 515 interactions.
DIPiDIP-12034N.
IntActiP27434. 11 interactions.
MINTiMINT-7012109.
STRINGi511145.b2516.

Proteomic databases

EPDiP27434.
PaxDbiP27434.
PRIDEiP27434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75569; AAC75569; b2516.
BAA16403; BAA16403; BAA16403.
GeneIDi946992.
KEGGiecj:JW2500.
eco:b2516.
PATRICi32120425. VBIEscCol129921_2615.

Organism-specific databases

EchoBASEiEB0015.
EcoGeneiEG10015. yfgA.

Phylogenomic databases

eggNOGiENOG4105HSZ. Bacteria.
COG1426. LUCA.
HOGENOMiHOG000276142.
InParanoidiP27434.
KOiK15539.
OMAiKLPGHTF.
OrthoDBiEOG65XN0H.

Enzyme and pathway databases

BioCyciEcoCyc:EG10015-MONOMER.
ECOL316407:JW2500-MONOMER.

Miscellaneous databases

PROiP27434.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
HAMAPiMF_02017. RodZ.
InterProiIPR001387. Cro/C1-type_HTH.
IPR025194. DUF4115.
IPR010982. Lambda_DNA-bd_dom.
IPR023690. RodZ.
[Graphical view]
PfamiPF13464. DUF4115. 1 hit.
PF13413. HTH_25. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence and characterization of the Escherichia coli genome between the ndk and gcpE genes."
    Baker J., Parker J.
    FEMS Microbiol. Lett. 121:293-296(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
    Strain: K12.
  5. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 158-243.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Sequence and characterization of the gcpE gene of Escherichia coli."
    Baker J., Franklin D.B., Parker J.
    FEMS Microbiol. Lett. 73:175-180(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-337.
  7. "Analysis of products of the Escherichia coli genomic genes and regulation of their expressions: an applicable procedure for genomic analysis of other microorganisms."
    Talukder A.A., Yanai S., Yamada M.
    Biosci. Biotechnol. Biochem. 58:117-120(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-55.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Determination of bacterial rod shape by a novel cytoskeletal membrane protein."
    Shiomi D., Sakai M., Niki H.
    EMBO J. 27:3081-3091(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DETERMINATION OF CELL SHAPE, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRODZ_ECOLI
AccessioniPrimary (citable) accession number: P27434
Secondary accession number(s): P76987, P77137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: March 16, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.