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Database: UniProt
Entry: H2J5F8_MARPK
LinkDB: H2J5F8_MARPK
Original site: H2J5F8_MARPK 
ID   H2J5F8_MARPK            Unreviewed;       233 AA.
AC   H2J5F8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000256|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000256|HAMAP-Rule:MF_01318};
GN   OrderedLocusNames=Marpi_1716 {ECO:0000313|EMBL:AEX86102.1};
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Marinitoga.
OX   NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX86102.1, ECO:0000313|Proteomes:UP000007161};
RN   [1] {ECO:0000313|EMBL:AEX86102.1, ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RX   PubMed=23045491; DOI=10.1128/JB.01430-12;
RA   Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA   Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT   "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT   Bacterium Marinitoga piezophila KA3.";
RL   J. Bacteriol. 194:5974-5975(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000256|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000256|ARBA:ARBA00010531, ECO:0000256|HAMAP-Rule:MF_01318,
CC       ECO:0000256|RuleBase:RU000659}.
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DR   EMBL; CP003257; AEX86102.1; -; Genomic_DNA.
DR   RefSeq; WP_014297173.1; NC_016751.1.
DR   AlphaFoldDB; H2J5F8; -.
DR   STRING; 443254.Marpi_1716; -.
DR   KEGG; mpz:Marpi_1716; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_0; -.
DR   OrthoDB; 9803740at2; -.
DR   Proteomes; UP000007161; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_uL1_bac-type.
DR   InterPro; IPR002143; Ribosomal_uL1.
DR   InterPro; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_uL1_CS.
DR   NCBIfam; TIGR01169; rplA_bact; 1.
DR   PANTHER; PTHR36427:SF3; 39S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR36427; 54S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007161};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_01318};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_01318}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01318}.
SQ   SEQUENCE   233 AA;  25649 MW;  8009082258F7AA72 CRC64;
     MSRHGKRYLE ARKLIDREKF YSLDEALELL PKIATAKFDE SVELHIILGI DPRKSDQQVR
     GNISLPHGTG KNVRVLVFAK GEKVKEALDA GADYAGSDEL IQKINEGWTD FDVAIATPDM
     MREIGRLGKV LGPRGLMPSP KGGTVTNDVA DAVKEFKAGK IEVRNDKTGN LHVAVGKKSF
     EPAKLKENIV EALQQIEKMR PSAAKGKFIR KVSLAPTMGP GMKINVSEFL TEK
//
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