ID A4A5F2_9GAMM Unreviewed; 308 AA.
AC A4A5F2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000256|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN Name=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN ORFNames=KT71_10357 {ECO:0000313|EMBL:EAQ99023.1};
OS Congregibacter litoralis KT71.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Congregibacter.
OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99023.1, ECO:0000313|Proteomes:UP000019205};
RN [1] {ECO:0000313|EMBL:EAQ99023.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99023.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT "Characterization of a marine gammaproteobacterium capable of aerobic
RT anoxygenic photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN [2] {ECO:0000313|EMBL:EAQ99023.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99023.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT "The photosynthetic apparatus and its regulation in the aerobic
RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL PLoS ONE 4:E4866-E4866(2009).
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42928, Rhea:RHEA-COMP:10286, Rhea:RHEA-COMP:10287,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; EC=2.1.1.199;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000256|ARBA:ARBA00010396, ECO:0000256|HAMAP-Rule:MF_01007}.
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:EAQ99023.1}.
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DR EMBL; AAOA02000003; EAQ99023.1; -; Genomic_DNA.
DR RefSeq; WP_008294507.1; NZ_CM002299.1.
DR AlphaFoldDB; A4A5F2; -.
DR STRING; 314285.KT71_10357; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_6; -.
DR OrthoDB; 9806637at2; -.
DR Proteomes; UP000019205; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.170; Putative methyltransferase TM0872, insert domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00006; 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH; 1.
DR PANTHER; PTHR11265:SF0; 12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11265; S-ADENOSYL-METHYLTRANSFERASE MRAW; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF81799; Putative methyltransferase TM0872, insert domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01007}; Reference proteome {ECO:0000313|Proteomes:UP000019205};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01007}.
FT BINDING 33..35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ SEQUENCE 308 AA; 34000 MW; 98D476E9F34D877A CRC64;
MAASHETVLL HEAVDALVGS PAGLYVDGTF GRGGHSREIL RRLDNQGRLF ACDKDEEAER
DAEELLAGDD RFSFARGSFA ALPAFLEERG LGAVDGILLD LGVSSPQLDQ AERGFSFQQD
GPLDMRMDRS RGESAADWIA AAPEQEIIDV LREYGEERYA RRIAAAIVKA RSEKPLTRTA
QLASIVSEAH PRWEKHKHPA TRSFQAIRIR VNRELDDLAE LLSLALSVLA VGGRLVVISF
HSLEDRLVKR HLRDMSRGPQ LPRDLPVRDV DVGVPMRLLG KAVRASDQEV AANPRSRSAI
MRCAEKIA
//
