ID G7Z834_AZOL4 Unreviewed; 568 AA.
AC G7Z834;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:CBS85588.1};
GN OrderedLocusNames=AZOLI_0174 {ECO:0000313|EMBL:CBS85588.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85588.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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|ARBA:ARBA00025604,
CC 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; FQ311868; CBS85588.1; -; Genomic_DNA.
DR RefSeq; WP_014246655.1; NC_016622.1.
DR AlphaFoldDB; G7Z834; -.
DR STRING; 862719.AZOLI_0174; -.
DR KEGG; ali:AZOLI_0174; -.
DR HOGENOM; CLU_015805_2_1_5; -.
DR OMA; SLNEFRY; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000005667; 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; cd05691; S1_RPS1_repeat_ec6; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 5.
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:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 30..96
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 114..180
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 201..269
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 286..356
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 373..443
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 460..529
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 568 AA; 62287 MW; 61DDAB98338707DB CRC64;
MAQSLARTVE KESFASLLEE SLGAAESLEG TVVKGRVVAV ENDMVTIDVG LKSEGRVALK
EFAVAGQPPE LKAGDTVEVY LERMEDKNGE AMLSREKAKR EEAWALLEKS FNDQTRVTGV
IFGRVKGGFT VDLSGAVAFL PGSQVDIRPV RDISPLLGTP QPFQILKMDR SRGNIVVSRR
AVLEESRAEA RSELVANLKE GQILQGVVKN ITDYGAFVDL GGVDGLLHVT DIAWRRINHP
SEALQIGQTV TVQVIRFNPE TQRISLGMKQ LEADPWEGVE AKYPVSAKFK GRVTNITDYG
AFVELEPGIE GLVHVSEMSW TKKNVHPGKI VSTSQEVEVM VLDVDPQKRR ISLGLKQCLD
NPWETFTDKF GPGTELEGEV KNITEFGLFV GLPGDIDGMV HMSDLDWNKS GEEAIAEYKK
GDRVKVKVLD VDVEKERISL GIKQLANDPF EAATAGLKKN EVVTCTVTQV TDGGIEVAVG
EGYTGFIRKS DLSRERSEQR PDRFAVGEKV DAKVTQIDRA SRRISLSIKA REMEEEKQAM
AEFGSSDSGA SLGDILGAAL KRKQQNDE
//