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Database: UniProt
Entry: Q5P7V1_AROAE
LinkDB: Q5P7V1_AROAE
Original site: Q5P7V1_AROAE 
ID   Q5P7V1_AROAE            Unreviewed;       591 AA.
AC   Q5P7V1;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:CAI06610.1};
GN   ORFNames=ebA903 {ECO:0000313|EMBL:CAI06610.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06610.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI06610.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI06610.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC       point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC       purine-rich sequence. {ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
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DR   EMBL; CR555306; CAI06610.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5P7V1; -.
DR   STRING; 76114.ebA903; -.
DR   KEGG; eba:ebA903; -.
DR   eggNOG; COG0539; Bacteria.
DR   HOGENOM; CLU_015805_2_1_4; -.
DR   Proteomes; UP000006552; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR   CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR   CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR   CDD; cd05689; S1_RPS1_repeat_ec4; 1.
DR   CDD; cd05691; S1_RPS1_repeat_ec6; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_bS1.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00717; rpsA; 1.
DR   PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR   PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:CAI06610.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          52..118
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          136..202
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          223..291
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          308..378
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          395..465
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          482..551
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   591 AA;  65493 MW;  1E60035F1EC9A151 CRC64;
     MFSDFQSSTG SRFRAAFGPS LFMTTATPVS DFQESFADLF EESLARQEMR SGEVITAEVV
     SIDHNFVVVN AGLKSESYVP IEEFRDDRGE LEVQVGDFVH VAIDALEDGY GETRLSREKA
     KRIAAWNDLE KALNEGSLVK GLISGRVKGG LTVMTNSIRA FLPGSLVDMR PVKDTSPYEG
     KEFEFKVIKL DRKRNNVVVS RRAVLEETMG EEREKLLANL KEGTVIKGIV KNITDYGAFV
     DLGGIDGLLH ITDLAWRRVR HPSEVLNVGD EIDAKVLKFD QEKNRVSLGL KQLGEDPWVG
     ISRRYPQGTR LFGKVTNITD YGAFVEVEQG IEGLVHVSEM DWTNKNIHPT KVVQLGDEVE
     VMILEIDEDR RRISLGMKQC MSNPWDDFAI NHKKGDKVRG QIKSITDFGV FIGLDGGIDG
     LVHLSDLSWS DTGEEAVRRF KKGDEVEAVV LAIDVERERI SLGVKQLEGD PFTNFIATHE
     KNSIVGGTVK SVEARGAVIA LNEDVEGYLR ASEAAAHRVD DLTTVLKEGQ EVEVMIINVD
     RKTRSINLSI RAKDQAEQSD AMQKFASDSS AASGTTNLGA LLKAKLNEQK Q
//
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