Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal recognition particle 54 kDa protein

Gene

srp54

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi107 – 114GTPUniRule annotation8
Nucleotide bindingi188 – 192GTPUniRule annotation5
Nucleotide bindingi247 – 250GTPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle 54 kDa proteinUniRule annotation
Short name:
SRP54UniRule annotation
Gene namesi
Name:srp54UniRule annotation
Ordered Locus Names:MJ0101
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

  • Note: The SRP-RNC complex is targeted to the cytoplasmic membrane.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001011771 – 451Signal recognition particle 54 kDa proteinAdd BLAST451

Proteomic databases

PRIDEiQ57565.

Interactioni

Subunit structurei

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. Archaeal SRP consists of a 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and SRP19.UniRule annotation

Protein-protein interaction databases

DIPiDIP-46442N.
STRINGi243232.MJ_0101.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Beta strandi18 – 20Combined sources3
Helixi28 – 40Combined sources13
Helixi45 – 51Combined sources7
Helixi53 – 59Combined sources7
Beta strandi60 – 62Combined sources3
Helixi70 – 86Combined sources17
Beta strandi97 – 99Combined sources3
Beta strandi103 – 106Combined sources4
Beta strandi109 – 112Combined sources4
Helixi115 – 128Combined sources14
Beta strandi131 – 134Combined sources4
Helixi143 – 145Combined sources3
Helixi148 – 153Combined sources6
Beta strandi158 – 160Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi167 – 169Combined sources3
Helixi172 – 177Combined sources6
Beta strandi183 – 188Combined sources6
Helixi196 – 205Combined sources10
Beta strandi208 – 210Combined sources3
Beta strandi213 – 220Combined sources8
Helixi221 – 226Combined sources6
Helixi227 – 235Combined sources9
Beta strandi242 – 247Combined sources6
Beta strandi249 – 251Combined sources3
Helixi256 – 264Combined sources9
Beta strandi269 – 272Combined sources4
Beta strandi275 – 280Combined sources6
Beta strandi281 – 283Combined sources3
Helixi286 – 293Combined sources8
Turni305 – 307Combined sources3
Turni308 – 311Combined sources4
Beta strandi312 – 315Combined sources4
Helixi318 – 321Combined sources4
Helixi327 – 334Combined sources8
Turni335 – 337Combined sources3
Helixi345 – 348Combined sources4
Helixi351 – 355Combined sources5
Helixi360 – 363Combined sources4
Helixi367 – 377Combined sources11
Helixi382 – 385Combined sources4
Helixi388 – 390Combined sources3
Helixi393 – 402Combined sources10
Helixi407 – 423Combined sources17
Turni424 – 427Combined sources4
Beta strandi434 – 436Combined sources3
Helixi437 – 445Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V3CX-ray2.50C/D3-427[»]
3NDBX-ray3.00B3-431[»]
4XCOX-ray2.90C/D304-451[»]
ProteinModelPortaliQ57565.
SMRiQ57565.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57565.

Family & Domainsi

Domaini

Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.UniRule annotation

Sequence similaritiesi

Belongs to the GTP-binding SRP family. SRP54 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01228. Archaea.
COG0541. LUCA.
InParanoidiQ57565.
KOiK03106.
OMAiKMGPMKQ.
PhylomeDBiQ57565.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q57565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDKLGENLN KALNKLKAAA FVDKKLIKEV IKDIQRALIQ ADVNVKLVLK
60 70 80 90 100
MSKEIERRAL EEKTPKGLSK KEHIIKIVYE ELVKLLGEEA KKLELNPKKQ
110 120 130 140 150
NVILLVGIQG SGKTTTAAKL ARYIQKRGLK PALIAADTYR PAAYEQLKQL
160 170 180 190 200
AEKIHVPIYG DETRTKSPVD IVKEGMEKFK KADVLIIDTA GRHKEEKGLL
210 220 230 240 250
EEMKQIKEIT NPDEIILVID GTIGQQAGIQ AKAFKEAVGE IGSIIVTKLD
260 270 280 290 300
GSAKGGGALS AVAETKAPIK FIGIGEGIDD LEPFDPKKFI SRLLGMGDLE
310 320 330 340 350
SLLEKAEDMV DEKTEESIDA IMRGKFTLNE LMTQLEAIEN MGSMKKILSM
360 370 380 390 400
IPGFGGAMPK ELSHLTEAKI KKYKVIISSM TKEERENPKI IKASRIRRIA
410 420 430 440 450
RGSGTTENDV REVLRYYETT KNAIDKLRKG KMLRIGGPLG QIMRQLMFKE

G
Length:451
Mass (Da):50,124
Last modified:November 1, 1997 - v1
Checksum:i5EEAF505FD227914
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98081.1.
PIRiE64312.
RefSeqiWP_010869593.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98081; AAB98081; MJ_0101.
GeneIDi1450940.
KEGGimja:MJ_0101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98081.1.
PIRiE64312.
RefSeqiWP_010869593.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V3CX-ray2.50C/D3-427[»]
3NDBX-ray3.00B3-431[»]
4XCOX-ray2.90C/D304-451[»]
ProteinModelPortaliQ57565.
SMRiQ57565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46442N.
STRINGi243232.MJ_0101.

Proteomic databases

PRIDEiQ57565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98081; AAB98081; MJ_0101.
GeneIDi1450940.
KEGGimja:MJ_0101.

Phylogenomic databases

eggNOGiarCOG01228. Archaea.
COG0541. LUCA.
InParanoidiQ57565.
KOiK03106.
OMAiKMGPMKQ.
PhylomeDBiQ57565.

Miscellaneous databases

EvolutionaryTraceiQ57565.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRP54_METJA
AccessioniPrimary (citable) accession number: Q57565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.