ID A0A060NQI5_9BURK Unreviewed; 265 AA.
AC A0A060NQI5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ABC-type molybdate transport system, periplasmic component {ECO:0000313|EMBL:BAO81174.1};
GN Name=modA {ECO:0000313|EMBL:BAO81174.1};
GN ORFNames=SRAA_1320 {ECO:0000313|EMBL:BAO81174.1};
OS Serpentinimonas raichei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO81174.1, ECO:0000313|Proteomes:UP000067461};
RN [1] {ECO:0000313|EMBL:BAO81174.1, ECO:0000313|Proteomes:UP000067461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:BAO81174.1,
RC ECO:0000313|Proteomes:UP000067461};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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DR EMBL; AP014568; BAO81174.1; -; Genomic_DNA.
DR RefSeq; WP_045531594.1; NZ_AP014568.1.
DR AlphaFoldDB; A0A060NQI5; -.
DR STRING; 1458425.SRAA_1320; -.
DR KEGG; cbaa:SRAA_1320; -.
DR HOGENOM; CLU_065520_3_1_4; -.
DR Proteomes; UP000067461; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005950; ModA.
DR NCBIfam; TIGR01256; modA; 1.
DR PANTHER; PTHR30632; MOLYBDATE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30632:SF0; SULFATE-BINDING PROTEIN; 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 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:UP000067461};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..265
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001587950"
FT BINDING 47
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 75
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 184
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 202
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 265 AA; 28423 MW; C8DF01D6C606A917 CRC64;
MPKPWSPLLR LWNRLHRLPL LLALALLPVM GHAQAQPIQL TVSAAASLTN AFNEIAAAFT
AQNPDVRVAL NVGASGALLQ QIDRGAPVDV FASADEFTMD LAQQRGLIVA AQRHNFTRNL
LVLAVPADSR LALASLADLR QEAVRRVAIG NPASVPVGRY TQSALEAAGL WPAVSAKAIY
TLNVRQSLNY VSRGEVEAAF VYATDAALMP ERVRVAFQVP TPTPIVYPIA PVARSNQPAA
AQRFVAFVLS PPAQAILQRH GFLPP
//
