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RS13_ACIB5
ID   RS13_ACIB5              Reviewed;         118 AA.
AC   B7IA17;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=AB57_3508;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
CC   -!- FUNCTION: Located at the top of the head of the 30S subunit, it
CC       contacts several helices of the 16S rRNA. In the 70S ribosome it
CC       contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit
CC       (bridge B1b), connecting the 2 subunits; these bridges are implicated
CC       in subunit movement. Contacts the tRNAs in the A and P-sites.
CC       {ECO:0000255|HAMAP-Rule:MF_01315}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose heterodimer
CC       with protein S19. Forms two bridges to the 50S subunit in the 70S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01315}.
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DR   EMBL; CP001182; ACJ42875.1; -; Genomic_DNA.
DR   RefSeq; WP_000090815.1; NC_011586.2.
DR   PDB; 6V39; EM; 3.04 A; m=1-118.
DR   PDB; 6V3A; EM; 2.82 A; m=1-118.
DR   PDB; 6V3B; EM; 2.91 A; m=1-118.
DR   PDB; 6V3E; EM; 4.40 A; m=1-118.
DR   PDB; 7M4U; EM; 2.71 A; m=1-118.
DR   PDB; 7M4W; EM; 2.55 A; m=1-118.
DR   PDB; 7M4X; EM; 2.66 A; m=1-118.
DR   PDB; 7M4Y; EM; 2.50 A; m=1-118.
DR   PDB; 7M4Z; EM; 2.92 A; m=1-118.
DR   PDB; 7RYF; EM; 2.65 A; m=1-118.
DR   PDB; 7RYG; EM; 2.38 A; m=1-118.
DR   PDB; 7RYH; EM; 2.43 A; m=1-118.
DR   PDBsum; 6V39; -.
DR   PDBsum; 6V3A; -.
DR   PDBsum; 6V3B; -.
DR   PDBsum; 6V3E; -.
DR   PDBsum; 7M4U; -.
DR   PDBsum; 7M4W; -.
DR   PDBsum; 7M4X; -.
DR   PDBsum; 7M4Y; -.
DR   PDBsum; 7M4Z; -.
DR   PDBsum; 7RYF; -.
DR   PDBsum; 7RYG; -.
DR   PDBsum; 7RYH; -.
DR   AlphaFoldDB; B7IA17; -.
DR   SMR; B7IA17; -.
DR   IntAct; B7IA17; 1.
DR   GeneID; 58193616; -.
DR   GeneID; 60752584; -.
DR   GeneID; 66395762; -.
DR   KEGG; abn:AB57_3508; -.
DR   HOGENOM; CLU_103849_1_2_6; -.
DR   OMA; YRGLRHK; -.
DR   Proteomes; UP000007094; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.910.10; -; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR   InterPro; IPR001892; Ribosomal_S13.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR019980; Ribosomal_S13_bac-type.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   PANTHER; PTHR10871:SF1; PTHR10871:SF1; 1.
DR   Pfam; PF00416; Ribosomal_S13; 2.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   TIGRFAMs; TIGR03631; uS13_bact; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..118
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_1000141204"
FT   REGION          92..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          3..6
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           15..18
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           27..37
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           50..61
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           67..83
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           86..93
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:7M4U"
SQ   SEQUENCE   118 AA;  13267 MW;  D06A3CA6C72A6107 CRC64;
     MARIAGVNIP DNKHAVISLT YIFGIGRHTA KNILAAVGIT ETTKIRELDD AQLDAIRAEV
     AKVPTEGDLR REISMNIKRL MDLGCYRGLR HRRSLPVRGQ RTKTNARTRK GPRKPIKK
 
 
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