ID B6BI32_SULGG Unreviewed; 245 AA.
AC B6BI32; H1FUZ1;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Molybdenum ABC transporter, periplasmic molybdate-binding protein {ECO:0000313|EMBL:EHP30185.1};
DE EC=3.6.3.29 {ECO:0000313|EMBL:EHP30185.1};
GN Name=modA2 {ECO:0000313|EMBL:EHP30185.1};
GN ORFNames=SMGD1_1661 {ECO:0000313|EMBL:EHP30185.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30185.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30185.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30185.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP30185.1}.
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DR EMBL; AFRZ01000001; EHP30185.1; -; Genomic_DNA.
DR RefSeq; WP_008336358.1; NZ_DS995286.1.
DR AlphaFoldDB; B6BI32; -.
DR STRING; 929558.SMGD1_1661; -.
DR PATRIC; fig|929558.5.peg.1652; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_1_0_7; -.
DR OrthoDB; 9785015at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030973; F:molybdate ion binding; IEA:InterPro.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR CDD; cd13539; PBP2_AvModA; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR044084; AvModA-like_subst-bd.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF14; TUNGSTATE_MOLYBDATE_CHROMATE-BINDING PROTEIN MODA; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR PIRSF; PIRSF004846; ModA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EHP30185.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004846-1};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR004846-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..245
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002842999"
FT BINDING 55
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 162
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 245 AA; 27047 MW; 619DD5A97CA5244B CRC64;
MKRLFILLLL GISLVNAGTI SIAVAANVSY AIEDLKKEFN KTNPETKVRV TLGSSGKLTA
QIKHGAPYQI FMSANMKYPQ ALYQEKIAIT EPVVYALGSL AILSNKKRDL SDGIYILQSK
EVSKVAIANP KTAPYGIAAM QAITNAKFED DVKSKFVYGE SISQTVSYAV TAADVGIIAK
SSLYSPNMSQ YKENINWISI DSKLYTPIQQ GIVMLKDDKE VKAFYDFILS DDAKKIFKEY
GYLLP
//
