ID A0ZBZ3_NODSP Unreviewed; 264 AA.
AC A0ZBZ3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Molybdenum ABC transporter, periplasmic molybdenum-binding protein ModA {ECO:0000313|EMBL:AHJ27556.1};
GN ORFNames=NSP_12160 {ECO:0000313|EMBL:AHJ27556.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ27556.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ27556.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ27556.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000256|ARBA:ARBA00009175}.
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DR EMBL; CP007203; AHJ27556.1; -; Genomic_DNA.
DR RefSeq; WP_006194957.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZBZ3; -.
DR STRING; 313624.NSP_12160; -.
DR PATRIC; fig|313624.11.peg.1216; -.
DR eggNOG; COG0725; Bacteria.
DR HOGENOM; CLU_065520_3_1_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR CDD; cd13537; PBP2_YvgL_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005950; ModA.
DR InterPro; IPR041879; YvgL-like_PBP2.
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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT BINDING 46
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 74
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 155
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 182
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
FT BINDING 200
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000256|PIRSR:PIRSR004846-1"
SQ SEQUENCE 264 AA; 28528 MW; FC5EEFD49A8D9A80 CRC64;
MNKKQILSLI GIAVTSFFLA IALPLINPTP LTAQPNINLL ISAAASMKDA LEEIQPLYQQ
SKPNVNIRYN FGASGALQQQ IEQGAPADIF ISAARSQVDA LEQKGLLVAG TRTNLANNRL
VLIVPNNTNS INSFFNLADA KIKRIALGEP RSVPAGQYAD QVLKKLGIFE KIKSKLVLAN
NVRQVLAAVE SGNADAGLVY ATDAKISNKV KVVVAADEKY HSAIIYPMAV IKRSKNIPAA
KEFLEFLSSN QAKTVLKKYG FIVN
//
