ID A0A1T2XGV2_9BACL Unreviewed; 491 AA.
AC A0A1T2XGV2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Protein adenylyltransferase SelO {ECO:0000256|HAMAP-Rule:MF_00692};
DE EC=2.7.7.108 {ECO:0000256|HAMAP-Rule:MF_00692};
GN Name=selO {ECO:0000256|HAMAP-Rule:MF_00692};
GN ORFNames=BVG16_08490 {ECO:0000313|EMBL:OPA79127.1};
OS Paenibacillus selenitireducens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1324314 {ECO:0000313|EMBL:OPA79127.1, ECO:0000313|Proteomes:UP000190188};
RN [1] {ECO:0000313|EMBL:OPA79127.1, ECO:0000313|Proteomes:UP000190188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES3-24 {ECO:0000313|EMBL:OPA79127.1,
RC ECO:0000313|Proteomes:UP000190188};
RA Xu D., Yao R., Zheng S.;
RT "Genome analysis of Paenibacillus selenitrireducens ES3-24.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Ser, Thr or Tyr residues of target proteins (AMPylation).
CC {ECO:0000256|HAMAP-Rule:MF_00692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein]
CC + diphosphate; Xref=Rhea:RHEA:58120, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15073, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:142516; EC=2.7.7.108; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00692};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00692};
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000256|ARBA:ARBA00009747,
CC ECO:0000256|HAMAP-Rule:MF_00692}.
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:OPA79127.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSZX01000003; OPA79127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T2XGV2; -.
DR STRING; 1324314.BVG16_08490; -.
DR OrthoDB; 9773505at2; -.
DR Proteomes; UP000190188; Unassembled WGS sequence.
DR GO; GO:0070733; F:AMPylase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR PANTHER; PTHR32057:SF14; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00692};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00692}; Reference proteome {ECO:0000313|Proteomes:UP000190188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00692}.
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 94..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 129..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ SEQUENCE 491 AA; 55008 MW; FE76DAFAAF31F48D CRC64;
MAKEKESIEA GWNFDNSYSR LPKILYTHLN PTPVSAPSLI VLNDPLAASL GLNVQALQSE
EGVSVFAGNR VPEGASPLAQ AYAGHQFGHF NLLGDGRALL ISEQITPSGE RYDIQLKGSG
ATPYSRRGDG RAALGPMLRE YIISEAMYAL GIPTTRSLAV VATGETIIRE TRLPGAILTR
VAASHLRVGT FEYVAHWGTD EDLRDLADYT LQRHYPGVDD SENRYLRLLQ EVIKRQAALI
AKWQLVGFIH GVMNTDNMAI SGETIDYGPC AFMNVYDPAT VFSSIDREGR YAYGNQPNIG
AWNLARFAET LLPLLHDDEE QAIHLAQDEI SNFSELYRRQ WLEGMRAKLG IFNEEQQDES
LIESLLDMMH KHGADYTNTF LALTFDQQEK SDLYGSDEFA QWHKRWRERL SRQQEPRSAS
HALMRSSNPA VIPRNHRVEA ALEAAVNQED YSVMEQLLDV LRNPYAHAPE QVEFAALPPQ
SDCTYQTFCG T
//
