ID A0A397L621_9FLAO Unreviewed; 417 AA.
AC A0A397L621;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=sulfate adenylyltransferase {ECO:0000256|ARBA:ARBA00012391};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
GN ORFNames=OE09_0021 {ECO:0000313|EMBL:RIA08212.1};
OS Flavobacteriaceae bacterium MAR_2010_72.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250029 {ECO:0000313|EMBL:RIA08212.1, ECO:0000313|Proteomes:UP000265779};
RN [1] {ECO:0000313|EMBL:RIA08212.1, ECO:0000313|Proteomes:UP000265779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_72 {ECO:0000313|EMBL:RIA08212.1,
RC ECO:0000313|Proteomes:UP000265779};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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:RIA08212.1}.
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DR EMBL; QXCW01000002; RIA08212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397L621; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000265779; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR CDD; cd04166; CysN_ATPS; 1.
DR CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR044138; CysN_II.
DR InterPro; IPR044139; CysN_NoDQ_III.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR NCBIfam; TIGR02034; CysN; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:RIA08212.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265779};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIA08212.1}.
FT DOMAIN 5..213
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 417 AA; 46962 MW; 0D3A5520D8237D78 CRC64;
MLDNNQLLRF TTAGSVDDGK STLIGRLLYD SKSIFEDQLE AIENTSKKKG HEGVDLALFT
DGLRDEREQG ITIDVAYRYF TTPKRKFIIA DTPGHIQYTR NMVTGASTAN AAIILVDARH
GVIEQTKRHA FIASLLQIPH VIVCVNKMDL VEYSEEAYNT VIDQFEKFSS KFLVKDIRFI
PISALDGDNV VNRSENMDWY LGAPLLHTLE TLHISSDINK IDARFPVQTV LRPQNDSHRD
YRGYAGRVSS GVFRPGDEVT ILPSGFTSKI KTIDTFEGEL EEAFAPMSVS ITLTDDIDIS
RGDMIVRSNN KAKVTQDVEV MLCWLHNNPA KPRAKYTIKH TSNEQKAMIK EVVYKYDINT
LERKTDDKDL GMNDISKVKI RTTKPLMIDS YRENRITGSI ILVDDSTNET VAAGMVV
//