MSRB_BACSU
ID MSRB_BACSU Reviewed; 143 AA.
AC P54155;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; Synonyms=yppQ;
GN OrderedLocusNames=BSU21680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of methionine sulfoxide reductase B using minimal
RT constraint strategy; Northeast structural genomics target SR10.";
RL Submitted (OCT-2006) to the PDB data bank.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01400};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01400}.
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DR EMBL; L77246; AAA96648.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14086.1; -; Genomic_DNA.
DR PIR; F69940; F69940.
DR RefSeq; NP_390051.1; NC_000964.3.
DR RefSeq; WP_003230813.1; NZ_JNCM01000036.1.
DR PDB; 2KZN; NMR; -; A=1-143.
DR PDB; 3E0O; X-ray; 2.60 A; A/B/C/D/E/F=1-143.
DR PDBsum; 2KZN; -.
DR PDBsum; 3E0O; -.
DR AlphaFoldDB; P54155; -.
DR BMRB; P54155; -.
DR SMR; P54155; -.
DR STRING; 224308.BSU21680; -.
DR PaxDb; P54155; -.
DR PRIDE; P54155; -.
DR EnsemblBacteria; CAB14086; CAB14086; BSU_21680.
DR GeneID; 939102; -.
DR KEGG; bsu:BSU21680; -.
DR PATRIC; fig|224308.179.peg.2369; -.
DR eggNOG; COG0229; Bacteria.
DR InParanoid; P54155; -.
DR OMA; DEQWRAE; -.
DR PhylomeDB; P54155; -.
DR BioCyc; BSUB:BSU21680-MON; -.
DR BRENDA; 1.8.4.12; 658.
DR EvolutionaryTrace; P54155; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..143
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_0000140262"
FT DOMAIN 5..126
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:3E0O"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2KZN"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2KZN"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2KZN"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3E0O"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3E0O"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3E0O"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3E0O"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:3E0O"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3E0O"
SQ SEQUENCE 143 AA; 16602 MW; EC29C9B017C68EED CRC64;
MAYNKEEKIK SLNRMQYEVT QNNGTEPPFQ NEYWDHKEEG LYVDIVSGKP LFTSKDKFDS
QCGWPSFTKP IEEEVEEKLD TSHGMIRTEV RSRTADSHLG HVFNDGPGPN GLRYCINSAA
LRFVPKHKLK EEGYESYLHL FNK
