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RS1H_BACSU
ID   RS1H_BACSU              Reviewed;         382 AA.
AC   P38494;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=30S ribosomal protein S1 homolog;
GN   Name=ypfD; Synonyms=jofD; OrderedLocusNames=BSU22880;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7704259; DOI=10.1099/13500872-141-2-311;
RA   Sorokin A.V., Serror P., Pujic P., Azevedo V., Ehrlich S.D.;
RT   "The Bacillus subtilis chromosome region encoding homologues of the
RT   Escherichia coli mssA and rpsA gene products.";
RL   Microbiology 141:311-319(1995).
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   DISRUPTION PHENOTYPE, AND ROLE IN SPORULATION.
RC   STRAIN=168;
RX   PubMed=14586115; DOI=10.1271/bbb.67.2245;
RA   Ohashi Y., Inaoka T., Kasai K., Ito Y., Okamoto S., Satsu H., Tozawa Y.,
RA   Kawamura F., Ochi K.;
RT   "Expression profiling of translation-associated genes in sporulating
RT   Bacillus subtilis and consequence of sporulation by gene inactivation.";
RL   Biosci. Biotechnol. Biochem. 67:2245-2253(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
CC   -!- FUNCTION: Plays a role in sporulation. {ECO:0000269|PubMed:14586115}.
CC   -!- DISRUPTION PHENOTYPE: Decreased sporulation at 37 and 47 degrees
CC       Celsius. {ECO:0000269|PubMed:14586115}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000305}.
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DR   EMBL; U11687; AAA85150.1; -; Genomic_DNA.
DR   EMBL; L47648; AAC83962.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14204.1; -; Genomic_DNA.
DR   PIR; B69935; B69935.
DR   RefSeq; NP_390169.1; NC_000964.3.
DR   RefSeq; WP_003230556.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P38494; -.
DR   IntAct; P38494; 1.
DR   MINT; P38494; -.
DR   STRING; 224308.BSU22880; -.
DR   iPTMnet; P38494; -.
DR   jPOST; P38494; -.
DR   PaxDb; P38494; -.
DR   PRIDE; P38494; -.
DR   DNASU; 938986; -.
DR   EnsemblBacteria; CAB14204; CAB14204; BSU_22880.
DR   GeneID; 938986; -.
DR   KEGG; bsu:BSU22880; -.
DR   PATRIC; fig|224308.179.peg.2495; -.
DR   eggNOG; COG0539; Bacteria.
DR   InParanoid; P38494; -.
DR   OMA; WQQFART; -.
DR   PhylomeDB; P38494; -.
DR   BioCyc; BSUB:BSU22880-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
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   Gene3D; 2.40.50.140; -; 4.
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; 2.
DR   Pfam; PF00575; S1; 4.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   PROSITE; PS50126; S1; 4.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding.
FT   CHAIN           1..382
FT                   /note="30S ribosomal protein S1 homolog"
FT                   /id="PRO_0000196026"
FT   DOMAIN          16..84
FT                   /note="S1 motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          102..167
FT                   /note="S1 motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          188..256
FT                   /note="S1 motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          273..342
FT                   /note="S1 motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
SQ   SEQUENCE   382 AA;  42402 MW;  270B82C27602BBBA CRC64;
     MTEEMNQIDV QVPEVGDVVK GIVTKVEDKH VDVEIINVKQ SGIIPISELS SLHVEKASDV
     VKVDDELDLK VTKVEDDALI LSKRAVDADR AWEDLEKKFE TKEVFEAEVK DVVKGGLVVD
     IGVRGFIPAS LVEAHFVEDF TDYKGKTLSL LVVELDRDKN RVILSHRAVV ESEQANKKQE
     LLQSLEVGSV LDGKVQRLTD FGAFVDIGGI DGLVHISQLS HSHVEKPSDV VEEGQEVKVK
     VLSVDRDNER ISLSIKDTLP GPWNQIGEKV KPGDVLEGTV QRLVSFGAFV EILPGVEGLV
     HISQISNKHI GTPHEVLEEG QTVKVKVLDV NENEERISLS MRELEETPKA DQEDYRQYQA
     KEETSTGFQL GDLIGDKLNK LK
 
 
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