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Database: UniProt
Entry: K6ZQE6_9ALTE
LinkDB: K6ZQE6_9ALTE
Original site: K6ZQE6_9ALTE 
ID   K6ZQE6_9ALTE            Unreviewed;       616 AA.
AC   K6ZQE6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=C427_3399 {ECO:0000313|EMBL:AGH45508.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH45508.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH45508.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH45508.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(2013).
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}.
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DR   EMBL; CP003837; AGH45508.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6ZQE6; -.
DR   KEGG; gps:C427_3399; -.
DR   PATRIC; fig|1129794.4.peg.3378; -.
DR   eggNOG; COG0397; Bacteria.
DR   HOGENOM; CLU_010245_3_0_6; -.
DR   OrthoDB; 9776281at2; -.
DR   Proteomes; UP000011864; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000011864};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00692}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        353
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT   BINDING         166..169
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         200..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ   SEQUENCE   616 AA;  70062 MW;  CF3B59E20A4EC944 CRC64;
     MFCIQTIISC GVWFFRSCAV FITPLAWSIF MTNQLPKVTS PSIVTLEDLA ELADYSLQDT
     LNCDPDAKEN GIDYLPRQVF TGHYVPVNPT PIEDPEYIAH SKHFFRELGF ADSMATSADF
     ISMFSGDLSQ LPKPMRKLGW ATGYALSIYG NEYVQQCPFQ TGNGYGDGRA VSVLEAVIQD
     QRWEMQLKGG GRTPYCRGAD GRAVLRSSIR EFLVQDHMHS LGVPTSRSLS LYVSKSENVK
     RPWYSEGSRS KDPDMLISEP VAISTRVAPS FIRVGQLELF GRRARKNEHP KAMQELEKIV
     LHAIEREYAD VIDNQLSTAE KVLMLACEFR SRLTSLVANW IRVGFCQGNF NSDNCSVGGF
     TLDYGPFGFC DVYDPHFQSW TGGGHHFSFM NQPVAAQQNF KSFCNALRPL LTSYQGTLQH
     EPSKKNSLQQ DYLQQLDEIQ DGFSNVMQAQ MEKMWAGKLG LSTFNKALFS ELESLMAQTP
     VDYTLFFREL SMLPENIAPL KKSFYKDSED MDLRWSEWLA KWKSLIASDN VAAPRSDDEI
     SRQMKLVNPK YILREWFVVP AYQQATAGNY ALVRELQKIM TQPYAEQSKE IEDKYYRLKP
     FEFFELGGTS YYSCSS
//
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