ID A0A1G7THL2_9PSED Unreviewed; 91 AA.
AC A0A1G7THL2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Periplasmic mercury ion-binding protein {ECO:0000256|RuleBase:RU361212};
GN Name=merP {ECO:0000256|RuleBase:RU361212};
GN ORFNames=SAMN05216603_101377 {ECO:0000313|EMBL:SDG34808.1};
OS Pseudomonas benzenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=556533 {ECO:0000313|EMBL:SDG34808.1, ECO:0000313|Proteomes:UP000199168};
RN [1] {ECO:0000313|Proteomes:UP000199168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8628 {ECO:0000313|Proteomes:UP000199168};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNCT01000001; SDG34808.1; -; Genomic_DNA.
DR RefSeq; WP_000732290.1; NZ_FNCT01000001.1.
DR AlphaFoldDB; A0A1G7THL2; -.
DR SMR; A0A1G7THL2; -.
DR STRING; 556533.SAMN05216603_101377; -.
DR GeneID; 83641737; -.
DR OrthoDB; 7205933at2; -.
DR Proteomes; UP000199168; 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 PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..91
FT /note="Periplasmic mercury ion-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011787020"
FT DOMAIN 22..88
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 91 AA; 9548 MW; 21EB0D79E9795069 CRC64;
MKKLFASLAI AAVVAPVWAA TQTVTLSVPG MTCSACPITV KKAISKVEGV SKVNVTFETR
EAVVTFDDAK TSVQKLTKAT EDAGYPSSVK K
//
