Reviewed, UniProtKB/Swiss-Prot P04129 (MERP_SHIFL)

Names and origin

Protein names

Recommended name:
    Mercuric transport protein periplasmic component
Alternative name(s):
    Periplasmic mercury ion-binding protein
    Mercury scavenger protein

Gene names

Name:

merP

Encoded on

Plasmid IncFII R100 (NR1)

Organism

Shigella flexneri

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	91 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (merA) via the merT protein.
Subunit structure	Monomer.
Subcellular location	Periplasm Probable.
Sequence similarities	Contains 1 HMA domain.

Ontologies

Keywords
Biological process	Mercuric resistance Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Mercury Metal-binding
Technical term	3D-structure Plasmid Transposable element
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro mercury ion transport Inferred from electronic annotation. Source: InterPro transposition Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro mercury ion binding Inferred from electronic annotation. Source: UniProtKB-KW mercury ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Chain

20 – 91

72

Mercuric transport protein periplasmic component

PRO_0000021679

Regions

Domain

23 – 89

67

HMA

Sites

Metal binding

33

1

Mercury Potential

Metal binding

36

1

Mercury Potential

Experimental info

Sequence conflict

51

1

S → T in AAB59076. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

91

Helix Strand Turn

Details...

Beta strand

22 – 27

6

Beta strand

33 – 36

4

Turn

37 – 39

3

Beta strand

52 – 56

5

Turn

57 – 60

4

Beta strand

61 – 66

6

Helix

73 – 81

9

Beta strand

88 – 90

3

Sequences

	Sequence		Length	Mass (Da)
	P04129-1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 822183AC323031A5	FASTA	91	9,414
	10 20 30 40 50 60 MKKLFASLAL AAAVAPVWAA TQTVTLAVPG MTCAACPITV KKALSKVEGV SKVDVGFEKR 70 80 90 EAVVTFDDTK ASVQKLTKAT ADAGYPSSVK Q

References

[1]	"Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the beginning of the operon including the regulatory region and the first two structural genes." Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M., Haberstroh L., Silver S. Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984) [PubMed: 6091128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The DNA sequence of the mercury resistance operon of the IncFII plasmid NR1." Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O., Wisdom S. J. Mol. Appl. Genet. 2:601-619(1984) [PubMed: 6530603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Transposon: Tn21.
[3]	"Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system." Steele R.A., Opella S.J. Biochemistry 36:6885-6895(1997) [PubMed: 9188683] [Abstract] Cited for: STRUCTURE BY NMR.
[4]	"NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance." Qian H., Sahlman L., Eriksson P.O., Hambraeus C., Edlund U., Sethson I. Biochemistry 37:9316-9322(1998) [PubMed: 9649312] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J01730 Genomic DNA. Translation: AAA92262.1.
K03089 Genomic DNA. Translation: AAB59076.1.

PIR

RGEBHD. A03556.
S09524.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFI	NMR	-	A	20-91	[»]
1AFJ	NMR	-	A	20-91	[»]
1DVW	NMR	-	A	25-42	[»]
2HQI	NMR	-	A	20-91	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001757. ATPase_P-typ_ion-transptr.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe_transpt.
IPR001802. HG_scavenger.
IPR011795. MerP.
[Graphical view]

PANTHER

PTHR11939. ATPase_P. 1 hit.

Pfam

PF00403. HMA. 1 hit.
[Graphical view]

PRINTS

PR00946. HGSCAVENGER.

TIGRFAMs

TIGR02052. MerP. 1 hit.

PROSITE

PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MERP_SHIFL

Accession

Primary (citable) accession number: P04129
Secondary accession number(s): P07042

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)