Entry bact:Q8KES9_CHLTE

ID   Q8KES9_CHLTE            Unreviewed;       428 AA.
AC   Q8KES9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   10-MAY-2017, entry version 97.
DE   RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|SAAS:SAAS00672440};
DE            EC=2.1.1.176 {ECO:0000256|SAAS:SAAS00672440};
GN   Name=sun {ECO:0000313|EMBL:AAM71845.1};
GN   OrderedLocusNames=CT0603 {ECO:0000313|EMBL:AAM71845.1};
OS   Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 /
OS   TLS).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM71845.1, ECO:0000313|Proteomes:UP000001007};
RN   [1] {ECO:0000313|EMBL:AAM71845.1, ECO:0000313|Proteomes:UP000001007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC   {ECO:0000313|Proteomes:UP000001007};
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., Deboy R., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.L., Yang F.,
RA   Holt I., Umayam L.A., Mason T., Brenner M., Shea T.P., Parksey D.,
RA   Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D.,
RA   Vamathevan J., Khouri H., White O., Gruber T.M., Ketchum K.A.,
RA   Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|SAAS:SAAS00672432}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC       rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC       rRNA. {ECO:0000256|SAAS:SAAS00672435}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00633808}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023,
CC       ECO:0000256|SAAS:SAAS00811926}.
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DR   EMBL; AE006470; AAM71845.1; -; Genomic_DNA.
DR   RefSeq; NP_661503.1; NC_002932.3.
DR   RefSeq; WP_010932290.1; NC_002932.3.
DR   ProteinModelPortal; Q8KES9; -.
DR   STRING; 194439.CT0603; -.
DR   EnsemblBacteria; AAM71845; AAM71845; CT0603.
DR   GeneID; 1006251; -.
DR   KEGG; cte:CT0603; -.
DR   PATRIC; 21399275; VBIChlTep116050_0561.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; HIGLYQL; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000001007; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001007};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001007};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811931};
KW   rRNA processing {ECO:0000256|SAAS:SAAS00633795};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811929};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925}.
FT   DOMAIN      169    428       SAM_MT_RSMB_NOP.
FT                                {ECO:0000259|PROSITE:PS51686}.
FT   ACT_SITE    378    378       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     282    282       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     309    309       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     325    325       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       246    399       ipfam:Methyltr_RsmB-F [T]
FT   MYHIT         1    125       ipfam:NusB [T]
FT   MYHIT       169    428       iprf:SAM_MT_RSMB_NOP [T]
SQ   SEQUENCE   428 AA;  47216 MW;  CBAEBAAEF8304345 CRC64;
     MTARELALRV LLELDGMRKS EELLNRMHEH AGLGKNDRAL AKELVAGTLK YRLQCDFIIA
     RFYRHDYAKA ATVLKHILRL GVYQLLRLDR VPKSAAVNES VKLARKFKGD HLARLVNGLL
     RNISKATIDL DAWTAEMPES KRLSILYSFP EWLAARWLMR YGPDATLAML AHGNLPPATG
     YRINRLKANP ETLLARPELS DAKRVADADG LDRFFFSKQF ALLEPLLKEG LVSVQNPAQG
     QACLMAAPEP GSTVFDMCAA PGGKSTFMAE LMENRGRIIA LDRTPAKVAR IASNASALGI
     TIIEPREGDA LTFDPGCAMD TILLDAPCTG TGVLGRRAEL RWRTTPEKLR ELAALQAAML
     DRAASLLRPG GVLLYATCSV EPEENELQTE AFLKRHPEFI AEASRLTLPG SHEGFDGGFA
     ARFRKTEG
//