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Database: UniProt
Entry: A0A1V6M1C0_9BACT
LinkDB: A0A1V6M1C0_9BACT
Original site: A0A1V6M1C0_9BACT 
ID   A0A1V6M1C0_9BACT        Unreviewed;       575 AA.
AC   A0A1V6M1C0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=BIY37_04490 {ECO:0000313|EMBL:OQD46198.1};
OS   Candidatus Brocadia sapporoensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=392547 {ECO:0000313|EMBL:OQD46198.1, ECO:0000313|Proteomes:UP000242219};
RN   [1] {ECO:0000313|EMBL:OQD46198.1, ECO:0000313|Proteomes:UP000242219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=40 {ECO:0000313|EMBL:OQD46198.1,
RC   ECO:0000313|Proteomes:UP000242219};
RX   PubMed=27932661;
RA   Ali M., Haroon M.F., Narita Y., Zhang L., Rangel Shaw D., Okabe S.,
RA   Saikaly P.E.;
RT   "Draft Genome Sequence of the Anaerobic Ammonium-Oxidizing Bacterium
RT   'Candidatus Brocadia sp. 40'.";
RL   Genome Announc. 4:e01377-16(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD46198.1}.
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DR   EMBL; MJUW02000052; OQD46198.1; -; Genomic_DNA.
DR   RefSeq; WP_070066629.1; NZ_MJUW02000052.1.
DR   AlphaFoldDB; A0A1V6M1C0; -.
DR   Proteomes; UP000242219; Unassembled WGS sequence.
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; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR   CDD; cd05688; S1_RPS1_repeat_ec3; 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   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; 3.
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:UP000242219};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OQD46198.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          47..110
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          128..193
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          214..282
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          299..369
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          386..456
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          474..543
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          549..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  64034 MW;  E2E611BF80D19DFC CRC64;
     MDRDFLKEYN VNLADIEREV EAIVGSADNK KKIESTYYDS IQNFEVGSVL KGRILSALGD
     NIVIDCGYKS EGMIPKFEFD DPSEIKIGDD VEVLLEAVED DSGLIKLSKR KADRIRGWER
     VIAKYKEGDI ITGRVTRKIK GGLLVDMGVP IFLPASQIDV KPPGDISQYI GQEVTCRILK
     IDESRQNIVV SRRKLIEEDR DKKKQGLLSE IAVGQTRKGL VKNIADFGAF IDLGGLDGLL
     HITDMSWGRI SHPSEMLAID DEVEVMILDI DKEKEKVALG LKQKSQNPWF LIDEKYPVGS
     RVKGQVVNIM SYGAFVKLET GIEGLVHISE MSWTRRINHP SEMVAIGDMV EVVVLKIDKE
     KEEISLSMKQ TEVNPWTVIE EKYPPGTKIK GRVRNLTNYG AFIEIEEGVD GLLHISDMSW
     ARKVGHPSEI VKKGDKVEAV VLSVDREKKR VALGLKQLSD DPWVKEIPEK YKVGDVITGK
     VTKLTNFGAF LELGKGIEGL LHISELSSEK VNNPADVVNI GDDLEVRVIR IEPEARKIGL
     SLKKMFGAEG RSEIPATPNE DSQKPSGDEA SAMNT
//
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