ID B7JAI3_ACIF2 Unreviewed; 128 AA.
AC B7JAI3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Small ribosomal subunit protein uS9 {ECO:0000256|HAMAP-Rule:MF_00532};
GN Name=rpsI {ECO:0000256|HAMAP-Rule:MF_00532,
GN ECO:0000313|EMBL:ACK79619.1};
GN OrderedLocusNames=AFE_3074 {ECO:0000313|EMBL:ACK79619.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK79619.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK79619.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000256|ARBA:ARBA00005251, ECO:0000256|HAMAP-Rule:MF_00532,
CC ECO:0000256|RuleBase:RU003815}.
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DR EMBL; CP001219; ACK79619.1; -; Genomic_DNA.
DR RefSeq; WP_009567384.1; NC_011761.1.
DR AlphaFoldDB; B7JAI3; -.
DR STRING; 243159.AFE_3074; -.
DR PaxDb; 243159-AFE_3074; -.
DR GeneID; 66434014; -.
DR KEGG; afr:AFE_3074; -.
DR eggNOG; COG0103; Bacteria.
DR HOGENOM; CLU_046483_2_1_6; -.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000754; Ribosomal_uS9.
DR InterPro; IPR023035; Ribosomal_uS9_bac/plastid.
DR InterPro; IPR020574; Ribosomal_uS9_CS.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR21569:SF1; 28S RIBOSOMAL PROTEIN S9, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001362};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00532};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00532}.
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 128 AA; 14464 MW; BC956A2F4A8F893D CRC64;
MEQYYGTGRR KSATARVYLR RGSGKIVINK RTLEDYFGRE TSRMVVMQPL ELTGHGGQFD
ILVNVNGGGA SGQAGAIRHG ITRALMVYDE TLRRPLRSAG FVTRDAREVE RKKVGKHKAR
RSHQFSKR
//
