MSRP_ECOLC
ID MSRP_ECOLC Reviewed; 334 AA.
AC B1IZU1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000255|HAMAP-Rule:MF_01206};
DE EC=1.8.5.- {ECO:0000255|HAMAP-Rule:MF_01206};
DE Flags: Precursor;
GN Name=msrP {ECO:0000255|HAMAP-Rule:MF_01206}; OrderedLocusNames=EcolC_1674;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC proteins containing methionine sulfoxide residues (Met-O), using
CC respiratory chain electrons. Thus protects these proteins from
CC oxidative-stress damage caused by reactive species of oxygen and
CC chlorine generated by the host defense mechanisms. MsrPQ is essential
CC for the maintenance of envelope integrity under bleach stress, rescuing
CC a wide series of structurally unrelated periplasmic proteins from
CC methionine oxidation, including the primary periplasmic chaperone SurA
CC and the lipoprotein Pal. The catalytic subunit MsrP is non-
CC stereospecific, being able to reduce both (R-) and (S-)
CC diastereoisomers of methionine sulfoxide. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:51296, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01206}.
CC Note=Is attached to the inner membrane when interacting with the MsrQ
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; CP000946; ACA77326.1; -; Genomic_DNA.
DR RefSeq; WP_000740094.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IZU1; -.
DR SMR; B1IZU1; -.
DR KEGG; ecl:EcolC_1674; -.
DR HOGENOM; CLU_045520_0_0_6; -.
DR OMA; WPYTEGL; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.420.10; -; 1.
DR HAMAP; MF_01206; MsrP; 1.
DR InterPro; IPR022867; MsrP.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..44
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT CHAIN 45..334
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT /id="PRO_5000314360"
FT BINDING 88
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 91..92
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 146
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 181
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 233
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 238
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 249..251
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ SEQUENCE 334 AA; 37383 MW; CB114F06534F30A8 CRC64;
MKKNQFLKES DVTAESVFFM KRRQVLKALG ISAAALSLPH AAHADLLSWF KGNDRPPAPA
GKPLEFSKPA AWQNNLPLTP ADKVSGYNNF YEFGLDKADP AANAGSLKTD PWTLKISGEV
AKPLTLDHDD LTRRFPLEER IYRMRCVEAW SMVVPWIGFP LHKLLALAEP TSNAKYVAFE
TIYAPEQMPG QQDRFIGGGL KYPYVEGLRL DEAMHPLTLM TVGVYGKALP PQNGAPVRLI
VPWKYGFKGI KSIVSIKLTR ERPPTTWNLA APDEYGFYAN VNPHVDHPRW SQATERFIGS
GGILDVQRQP TLLFNGYADQ VASLYRGLDL RENF
