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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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