YCAO_ECOLI
ID YCAO_ECOLI Reviewed; 586 AA.
AC P75838; Q9R2W0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ribosomal protein S12 methylthiotransferase accessory factor YcaO;
GN Name=ycaO; OrderedLocusNames=b0905, JW0888;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, INTERACTION WITH RIBOSOME, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=21169565; DOI=10.1074/mcp.m110.005199;
RA Strader M.B., Costantino N., Elkins C.A., Chen C.Y., Patel I.,
RA Makusky A.J., Choy J.S., Court D.L., Markey S.P., Kowalak J.A.;
RT "A proteomic and transcriptomic approach reveals new insight into beta-
RT methylthiolation of Escherichia coli ribosomal protein S12.";
RL Mol. Cell. Proteomics 10:M110.005199.01-M110.005199.10(2011).
CC -!- FUNCTION: Involved in beta-methylthiolation of ribosomal protein S12.
CC {ECO:0000269|PubMed:21169565}.
CC -!- SUBUNIT: Interacts with the ribosomal small subunit.
CC {ECO:0000269|PubMed:21169565}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows a decrease in the ratio of
CC methylthiolated to unmodified S12 and a decrease in transcription of a
CC subset of genes. {ECO:0000269|PubMed:21169565}.
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DR EMBL; U00096; AAC73991.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35640.2; -; Genomic_DNA.
DR PIR; H64829; H64829.
DR RefSeq; NP_415425.4; NC_000913.3.
DR RefSeq; WP_001295344.1; NZ_SSZK01000002.1.
DR PDB; 4Q84; X-ray; 2.64 A; A/B=1-586.
DR PDB; 4Q85; X-ray; 3.29 A; A/B/C/D/E/F/G/H=1-586.
DR PDB; 4Q86; X-ray; 2.25 A; A/B/C/D/E/F/G/H=1-586.
DR PDBsum; 4Q84; -.
DR PDBsum; 4Q85; -.
DR PDBsum; 4Q86; -.
DR AlphaFoldDB; P75838; -.
DR SMR; P75838; -.
DR BioGRID; 4260837; 37.
DR DIP; DIP-11470N; -.
DR IntAct; P75838; 8.
DR STRING; 511145.b0905; -.
DR jPOST; P75838; -.
DR PaxDb; P75838; -.
DR PRIDE; P75838; -.
DR EnsemblBacteria; AAC73991; AAC73991; b0905.
DR EnsemblBacteria; BAA35640; BAA35640; BAA35640.
DR GeneID; 66670819; -.
DR GeneID; 945509; -.
DR KEGG; ecj:JW0888; -.
DR KEGG; eco:b0905; -.
DR PATRIC; fig|1411691.4.peg.1371; -.
DR EchoBASE; EB3463; -.
DR eggNOG; COG1944; Bacteria.
DR HOGENOM; CLU_022530_1_0_6; -.
DR InParanoid; P75838; -.
DR OMA; FRRMFGN; -.
DR PhylomeDB; P75838; -.
DR BioCyc; EcoCyc:G6468-MON; -.
DR BioCyc; MetaCyc:G6468-MON; -.
DR PRO; PR:P75838; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047693; F:ATP diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IMP:EcoCyc.
DR InterPro; IPR003776; YcaO-like_dom.
DR InterPro; IPR041080; YcaO_C.
DR Pfam; PF02624; YcaO; 1.
DR Pfam; PF18381; YcaO_C; 1.
DR TIGRFAMs; TIGR00702; TIGR00702; 1.
DR PROSITE; PS51664; YCAO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..586
FT /note="Ribosomal protein S12 methylthiotransferase
FT accessory factor YcaO"
FT /id="PRO_0000144976"
FT DOMAIN 60..437
FT /note="YcaO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00999"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 189..211
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:4Q86"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:4Q85"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 478..492
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 498..514
FT /evidence="ECO:0007829|PDB:4Q86"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4Q85"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 534..544
FT /evidence="ECO:0007829|PDB:4Q86"
FT HELIX 564..582
FT /evidence="ECO:0007829|PDB:4Q86"
SQ SEQUENCE 586 AA; 65652 MW; 44CD903F9E73F503 CRC64;
MTQTFIPGKD AALEDSIARF QQKLSDLGFQ IEEASWLNPV PNVWSVHIRD KECALCFTNG
KGATKKAALA SALGEYFERL STNYFFADFW LGETIANGPF VHYPNEKWFP LTENDDVPEG
LLDDRLRAFY DPENELTGSM LIDLQSGNED RGICGLPFTR QSDNQTVYIP MNIIGNLYVS
NGMSAGNTRN EARVQGLSEV FERYVKNRII AESISLPEIP ADVLARYPAV VEAIETLEAE
GFPIFAYDGS LGGQYPVICV VLFNPANGTC FASFGAHPDF GVALERTVTE LLQGRGLKDL
DVFTPPTFDD EEVAEHTNLE THFIDSSGLI SWDLFKQDAD YPFVDWNFSG TTEEEFATLM
AIFNKEDKEV YIADYEHLGV YACRIIVPGM SDIYPAEDLW LANNSMGSHL RETILSLPGS
EWEKEDYLNL IEQLDEEGFD DFTRVRELLG LATGSDNGWY TLRIGELKAM LALAGGDLEQ
ALVWTEWTME FNSSVFSPER ANYYRCLQTL LLLAQEEDRQ PLQYLNAFVR MYGADAVEAA
SAAMSGEAAF YGLQPVDSDL HAFAAHQSLL KAYEKLQRAK AAFWAK
