ID A0A2P8C9W8_9BACT Unreviewed; 626 AA.
AC A0A2P8C9W8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Small subunit ribosomal protein S1 {ECO:0000313|EMBL:PSK81742.1};
GN ORFNames=CLV93_108143 {ECO:0000313|EMBL:PSK81742.1};
OS Prolixibacter denitrificans.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Prolixibacter.
OX NCBI_TaxID=1541063 {ECO:0000313|EMBL:PSK81742.1, ECO:0000313|Proteomes:UP000240621};
RN [1] {ECO:0000313|EMBL:PSK81742.1, ECO:0000313|Proteomes:UP000240621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27267 {ECO:0000313|EMBL:PSK81742.1,
RC ECO:0000313|Proteomes:UP000240621};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767}.
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:PSK81742.1}.
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DR EMBL; PYGC01000008; PSK81742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8C9W8; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000240621; Unassembled WGS sequence.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; 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; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF00575; S1; 6.
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 Ribonucleoprotein {ECO:0000313|EMBL:PSK81742.1};
KW Ribosomal protein {ECO:0000313|EMBL:PSK81742.1}.
FT DOMAIN 74..137
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 155..221
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 242..310
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 327..397
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 414..484
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 501..566
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 70364 MW; 8FB1E8128798FA43 CRC64;
MSENKENLEQ TEAVNQAAEE AKAEKVEAKK VTSKEADEDF DWDAFEGTSL EATGEKKDEM
TALYNDTLSV LQEKEVVDGK VISLNKREVV VDIGYKSDGI VSLNEFRYNP DLKVGDTVEV
YVESLEDQKG QLVLSHKKAR ALRSWDRVNA ALEKDEVITG YIKCRTKGGM IVDVFGIEAF
LPGSQIDVKP IRDYDIYVGK TMEFKVVKIN QEFRNVVVSH KALIEAELEQ QKKEIISKLE
KGQVLEGTVK NITSYGVFID LGGVDGLIHI TDLSWGRVSH PSEIVQLDQK INVVILDFDD
DKKRIALGLK QLTPHPWDNL SAELKVGDIV KGKVVVLADY GAFVEIAAGV EGLIHVSEMS
WSQHLRSAQD FLKVGDEVEA MILTLDREDR KMSLGIKQLK PDPWEKIDEK YSVGSKHTAR
VRNFTNFGVF VEIEEGVDGL IHISDLSWTK KIKHPSEFTS IGADIEVVVL DIDKDNRRLS
LGHKQLEENP WDVFETIFTV DSIHEGTVID IFDKGAVISL PYGVEGFATP RHLVKEDGSQ
VKLDEKLEFK VIEFSKSAKR IILSHSRVYE DVKKAEDNAK KRTATKQTQK GMKTVKDNLE
KTTLGDISDL AALKSKMEKD EKKDNE
//
