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GS13_BACSU
ID   GS13_BACSU              Reviewed;         130 AA.
AC   P80870; O05238;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=General stress protein 13;
DE            Short=GSP13;
GN   Name=yugI; OrderedLocusNames=BSU31390;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA   Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA   Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT   "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT   of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL   Microbiology 143:2769-2774(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-37.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [4]
RP   IDENTIFICATION IN RIBOSOME COMPLEX.
RC   STRAIN=168;
RX   PubMed=17163968; DOI=10.1111/j.1365-2958.2006.05513.x;
RA   Natori Y., Nanamiya H., Akanuma G., Kosono S., Kudo T., Ochi K.,
RA   Kawamura F.;
RT   "A fail-safe system for the ribosome under zinc-limiting conditions in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 63:294-307(2007).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=19152054; DOI=10.1007/s10858-009-9298-y;
RA   Yu W., Hu J., Yu B., Xia W., Jin C., Xia B.;
RT   "Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain
RT   related to cold shock proteins.";
RL   J. Biomol. NMR 43:255-259(2009).
CC   -!- SUBUNIT: Found in association with the 30S subunit of the ribosome.
CC       {ECO:0000269|PubMed:17163968}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation.
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DR   EMBL; Z93934; CAB07921.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15128.1; -; Genomic_DNA.
DR   PIR; H70010; H70010.
DR   RefSeq; NP_391017.1; NC_000964.3.
DR   RefSeq; WP_003228864.1; NZ_JNCM01000033.1.
DR   PDB; 2K4K; NMR; -; A=1-130.
DR   PDBsum; 2K4K; -.
DR   AlphaFoldDB; P80870; -.
DR   BMRB; P80870; -.
DR   SMR; P80870; -.
DR   STRING; 224308.BSU31390; -.
DR   jPOST; P80870; -.
DR   PaxDb; P80870; -.
DR   PRIDE; P80870; -.
DR   EnsemblBacteria; CAB15128; CAB15128; BSU_31390.
DR   GeneID; 938849; -.
DR   KEGG; bsu:BSU31390; -.
DR   PATRIC; fig|224308.179.peg.3403; -.
DR   eggNOG; COG1098; Bacteria.
DR   InParanoid; P80870; -.
DR   OMA; HDIAKIG; -.
DR   PhylomeDB; P80870; -.
DR   BioCyc; BSUB:BSU31390-MON; -.
DR   EvolutionaryTrace; P80870; -.
DR   PRO; PR:P80870; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   DisProt; DP00809; -.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR10724:SF7; PTHR10724:SF7; 1.
DR   Pfam; PF00575; S1; 1.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50126; S1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..130
FT                   /note="General stress protein 13"
FT                   /id="PRO_0000083862"
FT   DOMAIN          8..77
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   REGION          76..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        30
FT                   /note="E -> W (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..19
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          22..28
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          57..66
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   HELIX           77..81
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2K4K"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:2K4K"
SQ   SEQUENCE   130 AA;  14283 MW;  DC047C02873AB4B9 CRC64;
     MAAKFEVGSV YTGKVTGLQA YGAFVALDEE TQGLVHISEV THGFVKDINE HLSVGDEVQV
     KVLAVDEEKG KISLSIRATQ AAPEKKESKP RKPKAAQVSE EASTPQGFNT LKDKLEEWIE
     MSNRKDLIKK
 
 
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