ID C0N3E0_9GAMM Unreviewed; 83 AA.
AC C0N3E0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Periplasmic mercury ion-binding protein {ECO:0000256|RuleBase:RU361212};
GN Name=merP {ECO:0000256|RuleBase:RU361212,
GN ECO:0000313|EMBL:EEF80699.1};
GN ORFNames=MDMS009_638 {ECO:0000313|EMBL:EEF80699.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF80699.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF80699.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF80699.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
CC -!- FUNCTION: Involved in mercury resistance. Acts as a mercury scavenger
CC that specifically binds to a mercuric ion in the periplasm and probably
CC passes it to the cytoplasmic mercuric reductase MerA via the mercuric
CC transport protein MerT. {ECO:0000256|RuleBase:RU361212}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU361212}.
CC -!- SIMILARITY: Belongs to the MerP family.
CC {ECO:0000256|ARBA:ARBA00005938}.
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DR EMBL; GG657889; EEF80699.1; -; Genomic_DNA.
DR AlphaFoldDB; C0N3E0; -.
DR HOGENOM; CLU_134973_2_1_6; -.
DR Proteomes; UP000004679; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0045340; F:mercury ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015097; F:mercury ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR011795; MerP.
DR InterPro; IPR001802; MerP/CopZ.
DR NCBIfam; TIGR02052; MerP; 1.
DR Pfam; PF00403; HMA; 1.
DR PRINTS; PR00946; HGSCAVENGER.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW Mercuric resistance {ECO:0000256|RuleBase:RU361212};
KW Mercury {ECO:0000256|RuleBase:RU361212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361212};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU361212};
KW Reference proteome {ECO:0000313|Proteomes:UP000004679};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 8..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 83 AA; 8547 MW; F15E65D6F7222558 CRC64;
MPALAAQQTV TLSVPGMTCP ACPFTVKAAL NKVNGVMQVD VSYPAREAVV TFDGTLTSVE
ALTQATTNAG YPSSPTASEE DPE
//
