ID A0A0B3VY45_9FIRM Unreviewed; 498 AA.
AC A0A0B3VY45;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=QX51_07245 {ECO:0000313|EMBL:KHS57619.1};
OS Terrisporobacter othiniensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Terrisporobacter.
OX NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS57619.1, ECO:0000313|Proteomes:UP000031189};
RN [1] {ECO:0000313|EMBL:KHS57619.1, ECO:0000313|Proteomes:UP000031189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-306576 {ECO:0000313|EMBL:KHS57619.1,
RC ECO:0000313|Proteomes:UP000031189};
RA Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M., Justesen U.S.;
RT "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated from the
RT blood culture of a bacteremia patient.";
RL Submitted (DEC-2014) 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:KHS57619.1}.
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DR EMBL; JWHR01000068; KHS57619.1; -; Genomic_DNA.
DR RefSeq; WP_039679238.1; NZ_JWHR01000068.1.
DR AlphaFoldDB; A0A0B3VY45; -.
DR STRING; 1577792.QX51_07245; -.
DR OrthoDB; 9773505at2; -.
DR Proteomes; UP000031189; 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:UP000031189};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00692}.
FT ACT_SITE 264
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 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 137..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ SEQUENCE 498 AA; 56918 MW; 001292AA0BD1BBCB CRC64;
MSEGKQINNI GWNFHNTYKD LPKPFYSEIK LSPVRKPELI ILNEPLAKAL NLNVEALKSK
EGVEILAGNK KAEGGACIAQ AYSGHQFGHF TMLGDGRAVL IGEQKVDTGI NITGESYKKF
DIQLKGSGRT PYSRGGDGRA VLGPMLREYI ISEAMYNLKI PTTRSLAVVK TGEKVYREYV
KEGAILTRVA SSHLRFGTFE YASNYLGKEE VKKLADYAIE THYPYVRNDE NKYLSFLKEV
IKAHASLVSK WLCVGFIHGV MNTDNMTISG ESIDYGPCAF MNTYDPDTVF SSIDVQGRYA
YKNQPSMASW NICRLAEALL PLINEDVDVA IDLAQKEIFK FSDLHFKYWF SQMRNKLGFF
NEEPMDKAII EDLLSMMEKY KEDYTNTFVS LTYRKNMNSG MFATSEFTNW HKNWQERLER
QEESIDEAYE LMKKSNPVVI PRNHRVEEAL KSADNGDFTV MEKLLSILSN PYEYKEEMDE
YTELAEPSDL PYRTYCGT
//
