ID K0CHT6_ALCDB Unreviewed; 559 AA.
AC K0CHT6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:AFT71242.1};
GN OrderedLocusNames=B5T_02974 {ECO:0000313|EMBL:AFT71242.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71242.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71242.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT71242.1; -; Genomic_DNA.
DR RefSeq; WP_014995308.1; NC_018691.1.
DR AlphaFoldDB; K0CHT6; -.
DR STRING; 930169.B5T_02974; -.
DR KEGG; adi:B5T_02974; -.
DR PATRIC; fig|930169.3.peg.2934; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_1_6; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000006286; 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:UP000006286};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:AFT71242.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 21..87
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 105..171
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 192..260
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 277..347
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 364..434
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 451..520
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 559 AA; 61850 MW; 04899FCCA9CB45A6 CRC64;
MTESFAELFE ESLKDLDVAR GSIIRGTVVA IDSDWVVVNA GLKSEGIISR DEFISESGEL
EIAEGDEVEV AVDAIDDGMG FTRLSREKAK RAEVWGELEV AFDKDEIVKG HISGKVKGGF
TVDIGPIRAF LPGSLVDIRP VRDVTHLEGK DLDFKVIKLD PKRNNVVVSR RAVMEAEHSA
EREALLESLQ EGMVVKGIVK NLTDYGAFVD LGGIDGLLHI TDMAWKRIKH PSEIVEVGQE
IEVKVLKFDR EKMRVSLGLK QLGEDPWHDI VQKYPEGARV KARVTNLTDY GCFAEIEEGV
EGLVHVSEMD WTNKNIHPSK VVEIGDEVEV MILDIDEDRR RISLGIKQCL SNPWEAFATN
YQKGDRISGK IKSITDFGIF IGLEGGIDGL VHLSDISWEE AGEDAVRNFN KGDELETVVL
SIDAERERIS LGIKQLTDDP FAQYVAANEK GSIVKGTVKA VDAKGATVEL AENVEGYLRA
SEISRDRIND ASQVLNVGDE VEGRITNIDR KNRSINVSVR AKDQVQDREA MDNLQGQDAN
APKTIGDLIK QQMENSNES
//
