SRP19_ARCFU
ID SRP19_ARCFU Reviewed; 104 AA.
AC O29010;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Signal recognition particle 19 kDa protein {ECO:0000255|HAMAP-Rule:MF_00305};
DE Short=SRP19 {ECO:0000255|HAMAP-Rule:MF_00305};
GN Name=srp19 {ECO:0000255|HAMAP-Rule:MF_00305}; OrderedLocusNames=AF_1258;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10684931; DOI=10.1093/nar/28.6.1365;
RA Bhuiyan S.H., Gowda K., Hotokezaka H., Zwieb C.;
RT "Assembly of archaeal signal recognition particle from recombinant
RT components.";
RL Nucleic Acids Res. 28:1365-1373(2000).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11041851; DOI=10.1021/bi001180s;
RA Diener J.L., Wilson C.;
RT "Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition
RT particle.";
RL Biochemistry 39:12862-12874(2000).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=11916385; DOI=10.1006/jmbi.2002.5411;
RA Pakhomova O.N., Deep S., Huang Q., Zwieb C., Hinck A.P.;
RT "Solution structure of protein SRP19 of Archaeoglobus fulgidus signal
RT recognition particle.";
RL J. Mol. Biol. 317:145-158(2002).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Binds directly to 7S RNA and
CC mediates binding of the 54 kDa subunit of the SRP. {ECO:0000255|HAMAP-
CC Rule:MF_00305, ECO:0000269|PubMed:10684931,
CC ECO:0000269|PubMed:11041851}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. Archaeal SRP consists of a
CC 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and
CC SRP19. {ECO:0000255|HAMAP-Rule:MF_00305, ECO:0000269|PubMed:10684931,
CC ECO:0000269|PubMed:11041851}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00305,
CC ECO:0000269|PubMed:10684931, ECO:0000269|PubMed:11041851}.
CC -!- SIMILARITY: Belongs to the SRP19 family. {ECO:0000255|HAMAP-
CC Rule:MF_00305}.
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DR EMBL; AE000782; AAB89988.1; -; Genomic_DNA.
DR PIR; A69407; A69407.
DR RefSeq; WP_010878753.1; NC_000917.1.
DR PDB; 1KVN; NMR; -; A=1-104.
DR PDB; 1KVV; NMR; -; A=1-104.
DR PDBsum; 1KVN; -.
DR PDBsum; 1KVV; -.
DR AlphaFoldDB; O29010; -.
DR BMRB; O29010; -.
DR SMR; O29010; -.
DR STRING; 224325.AF_1258; -.
DR PRIDE; O29010; -.
DR EnsemblBacteria; AAB89988; AAB89988; AF_1258.
DR GeneID; 24794861; -.
DR KEGG; afu:AF_1258; -.
DR eggNOG; arCOG01217; Archaea.
DR HOGENOM; CLU_169299_1_0_2; -.
DR OMA; VIWPAYL; -.
DR OrthoDB; 121943at2157; -.
DR PhylomeDB; O29010; -.
DR EvolutionaryTrace; O29010; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 3.30.56.30; -; 1.
DR HAMAP; MF_00305; SRP19; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR InterPro; IPR036521; SRP19-like_sf.
DR InterPro; IPR022938; SRP19_arc-type.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Signal recognition particle.
FT CHAIN 1..104
FT /note="Signal recognition particle 19 kDa protein"
FT /id="PRO_0000135214"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1KVN"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1KVN"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1KVN"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1KVN"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1KVN"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1KVN"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1KVN"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1KVN"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1KVN"
FT HELIX 75..94
FT /evidence="ECO:0007829|PDB:1KVN"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1KVN"
SQ SEQUENCE 104 AA; 12405 MW; 72D5DDABB4E89E64 CRC64;
MKECVVWTVN LDSKKSRAEG RRIPRRFAVP NVKLHELVEA CKELGLKFRA EEKKYPKSWW
EEGGRVVVEK RGTKTKLMIE LARKIAEIRE QKREQKKDKK KKKK
