ID A0A377R0J4_9NEIS Unreviewed; 515 AA.
AC A0A377R0J4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401};
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE Includes:
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=msrAB {ECO:0000313|EMBL:STR00525.1};
GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401}, msrB
GN {ECO:0000256|HAMAP-Rule:MF_01400};
GN ORFNames=NCTC13336_00734 {ECO:0000313|EMBL:STR00525.1};
OS Kingella potus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=265175 {ECO:0000313|EMBL:STR00525.1, ECO:0000313|Proteomes:UP000254293};
RN [1] {ECO:0000313|EMBL:STR00525.1, ECO:0000313|Proteomes:UP000254293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13336 {ECO:0000313|EMBL:STR00525.1,
RC ECO:0000313|Proteomes:UP000254293};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC {ECO:0000256|HAMAP-Rule:MF_01401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001063, ECO:0000256|HAMAP-
CC Rule:MF_01401};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001497, ECO:0000256|HAMAP-
CC Rule:MF_01401};
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_01401}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_01400}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00008076}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR EMBL; UGJJ01000001; STR00525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377R0J4; -.
DR OrthoDB; 4174719at2; -.
DR Proteomes; UP000254293; Unassembled WGS sequence.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR HAMAP; MF_01400; MsrB; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00401; msrA; 1.
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; PF01625; PMSR; 1.
DR Pfam; PF08534; Redoxin; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51790; MSRB; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000254293};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..515
FT /note="Multifunctional fusion protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016787576"
FT DOMAIN 27..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 376..499
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
FT ACT_SITE 488
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 515 AA; 57026 MW; DB88F6739FFBDDF5 CRC64;
MDKFWKPVFI AAAAAAGVAF FIPHSGAAQA APVPQMLAQL QDPQGRPAPR LDKNKPTLVK
FWASWCPLCL SELGHTEKWT QDKRFQAANL ITVASPGFLG EKKDGDFQKW YAGLNYPKLP
VVADNGGTIA QSLNVRVYPS WAVLDKNGNV ARIVKGSINE AQALALIDNP EADIGRLKTQ
FNTQDKAKVK PMNTKTIYLA GGCFWGLEAY FQRIDGVADA VSGYANGGTK NPSYQDVINN
SGHAETVKVT YDADKLSLDD ILQYYFRVID PTSLNKQGND RGIQYRTGVY YTDPAEKAVI
EKAFAREQKK YSQPVVVENQ PLQNFYEAEE YHQDYLIKNP NGYCHIDIRK ADEPLPGKAA
PQGKGFNAAS YHKPSDEELR RRLTREQYEV TQHAATEYAF SHEYDHLFKP GIYVDIVSGE
PLFSSADKYD SGCGWPSFTK PIEAAAVTEH SDTSYNMVRT EVRSRAADSH LGHVFPDGPK
DKGGLRYCIN GASLKFVPLA EMDAAGYGAL KNTVK
//
