ID A0A0K8MXE2_9CHLR Unreviewed; 323 AA.
AC A0A0K8MXE2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000256|HAMAP-Rule:MF_01206};
DE EC=1.8.5.- {ECO:0000256|HAMAP-Rule:MF_01206};
GN Name=msrP {ECO:0000256|HAMAP-Rule:MF_01206};
GN ORFNames=LARV_03723 {ECO:0000313|EMBL:GAP15928.1};
OS Longilinea arvoryzae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Longilinea.
OX NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP15928.1};
RN [1] {ECO:0000313|EMBL:GAP15928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOME-1 {ECO:0000313|EMBL:GAP15928.1};
RA Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Anaerolineaceae (Chloroflexi).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized cell envelope
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. MsrPQ is essential for the maintenance of envelope integrity
CC under bleach stress, rescuing a wide series of structurally unrelated
CC cell envelope proteins from methionine oxidation. The catalytic subunit
CC MsrP is non-stereospecific, being able to reduce both (R-) and (S-)
CC diastereoisomers of methionine sulfoxide. {ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01206};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01206};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01206};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01206}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000256|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; DF967973; GAP15928.1; -; Genomic_DNA.
DR RefSeq; WP_075075327.1; NZ_DF967973.1.
DR AlphaFoldDB; A0A0K8MXE2; -.
DR STRING; 360412.LARV_03723; -.
DR OrthoDB; 9778777at2; -.
DR Proteomes; UP000055060; Unassembled WGS sequence.
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; Oxidoreductase, molybdopterin-binding domain; 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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43032; PROTEIN-METHIONINE-SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR43032:SF3; PROTEIN-METHIONINE-SULFOXIDE REDUCTASE CATALYTIC SUBUNIT MSRP; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01206};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|HAMAP-
KW Rule:MF_01206};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01206}; Reference proteome {ECO:0000313|Proteomes:UP000055060};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01206}.
FT DOMAIN 106..261
FT /note="Oxidoreductase molybdopterin-binding"
FT /evidence="ECO:0000259|Pfam:PF00174"
FT BINDING 86
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 89..90
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 144
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 179
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 227
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 232
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
FT BINDING 243..245
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01206"
SQ SEQUENCE 323 AA; 35828 MW; A96C438F44E91809 CRC64;
MKTYRSQSAP PAAHEITPEH VYLNRRQFMK LGAAAVSLAA LAACAPLGSN AGPTLNAATP
SANEITPTPT MLPDTLTDFE AITNYNNFYE YSVDKQAVAQ LSKDLRTSPW TVEVGGLVTN
PKTYGVEDLT HLFPPEERIY RLRCVEAWSM VIPWLGFPLA SLLKAVEPTG DAKYVRFVTL
MDPSQMPGES DPSYPWPYQE GLRLDEAMHP LTILSTGLYG KALLPQNGAP IRLVVPWKYG
FKSIKSIIKI ELVAEQPATL WSSIAPNEYG FYANVNPDVP HPRWSQASER RIGELTRRPT
YLFNGYAADV AGLYAGMDLK KEY
//
