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Database: UniProt
Entry: L0AIW3_NATGS
LinkDB: L0AIW3_NATGS
Original site: L0AIW3_NATGS 
ID   L0AIW3_NATGS            Unreviewed;       137 AA.
AC   L0AIW3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400,
GN   ECO:0000313|EMBL:PLK19668.1};
GN   OrderedLocusNames=Natgr_2211 {ECO:0000313|EMBL:AFZ73389.1};
GN   ORFNames=C490_09208 {ECO:0000313|EMBL:ELY68585.1}, CYV19_13685
GN   {ECO:0000313|EMBL:PLK19668.1};
OS   Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS   104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronobacterium.
OX   NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ73389.1, ECO:0000313|Proteomes:UP000010468};
RN   [1] {ECO:0000313|Proteomes:UP000010468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC   {ECO:0000313|Proteomes:UP000010468};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFZ73389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:AFZ73389.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY68585.1, ECO:0000313|Proteomes:UP000011613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:ELY68585.1,
RC   ECO:0000313|Proteomes:UP000011613};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:PLK19668.1, ECO:0000313|Proteomes:UP000234484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:PLK19668.1,
RC   ECO:0000313|Proteomes:UP000234484};
RC   TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK19668.1};
RA   Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA   Huang J.;
RT   "The characterization of oligonucleotides binding to NgAgo.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:50058; EC=1.8.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001795, ECO:0000256|HAMAP-
CC         Rule:MF_01400};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01400};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC       structural integrity of the protein. {ECO:0000256|HAMAP-Rule:MF_01400};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR   EMBL; CP003377; AFZ73389.1; -; Genomic_DNA.
DR   EMBL; AOIC01000070; ELY68585.1; -; Genomic_DNA.
DR   EMBL; PKKI01000044; PLK19668.1; -; Genomic_DNA.
DR   RefSeq; WP_005579268.1; NZ_PKKI01000044.1.
DR   AlphaFoldDB; L0AIW3; -.
DR   STRING; 797304.Natgr_2211; -.
DR   GeneID; 14208078; -.
DR   KEGG; nge:Natgr_2211; -.
DR   PATRIC; fig|797304.7.peg.1856; -.
DR   eggNOG; arCOG02815; Archaea.
DR   HOGENOM; CLU_031040_8_5_2; -.
DR   Proteomes; UP000010468; Chromosome.
DR   Proteomes; UP000011613; Unassembled WGS sequence.
DR   Proteomes; UP000234484; Unassembled WGS sequence.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR   PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B3; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01400};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000010468};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01400}.
FT   DOMAIN          16..137
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ   SEQUENCE   137 AA;  15593 MW;  9BE391A811C39FB7 CRC64;
     MDHEPADTDQ DLPETDEQWR ERLDDEEYRI LREAGTETPF SGEYVDHKDD GSYACVGCGV
     ELFDSETKFD SGCGWPSFYD VDDDRIETRP DTSHGMRRTE ILCAECGGHL GHVFEDGPEP
     TGKRYCINSV ALEFDEE
//
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