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Database: UniProt
Entry: A0A431W4C5_9DEIO
LinkDB: A0A431W4C5_9DEIO
Original site: A0A431W4C5_9DEIO 
ID   A0A431W4C5_9DEIO        Unreviewed;       335 AA.
AC   A0A431W4C5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Zinc ABC transporter substrate-binding protein {ECO:0000313|EMBL:RTR30243.1};
GN   ORFNames=EJ104_01665 {ECO:0000313|EMBL:RTR30243.1};
OS   Deinococcus radiophilus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=32062 {ECO:0000313|EMBL:RTR30243.1, ECO:0000313|Proteomes:UP000277766};
RN   [1] {ECO:0000313|EMBL:RTR30243.1, ECO:0000313|Proteomes:UP000277766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27603 {ECO:0000313|EMBL:RTR30243.1,
RC   ECO:0000313|Proteomes:UP000277766};
RA   Maclea K.S., Maynard C.R.;
RT   "Deinococcus radiophilus ATCC 27603 genome sequencing and assembly.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000256|RuleBase:RU003512}.
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:RTR30243.1}.
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DR   EMBL; RXPE01000002; RTR30243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A431W4C5; -.
DR   OrthoDB; 9810636at2; -.
DR   Proteomes; UP000277766; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_PsaA-like.
DR   InterPro; IPR006127; ZnuA-like.
DR   PANTHER; PTHR42953; HIGH-AFFINITY ZINC UPTAKE SYSTEM PROTEIN ZNUA-RELATED; 1.
DR   PANTHER; PTHR42953:SF1; MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN; 1.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003512}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..335
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018992615"
FT   REGION          136..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  34770 MW;  2B5CFA3976D21905 CRC64;
     MKTRRFSIVL LSALLGACAA PAEQDAVAPA PQTTAAAPAS VDPQGGGLHV SATTSVMADL
     VRQAGGDRVQ VTSLLPLGAS PHTFDPTPQT IRELSGAQAL FSNGSGLEGW LGSLSGAASE
     VPTYALTEGL ALRVAEEEGD QPHSDHSDHD HGEYDPHAWL DPQLAAGYVD RAAAVLAELD
     PAGEGIYRAN AAAYREQLAE LEAYGQQRFE ALPAEARRVV TDHHALGYFA ERFGLEVVGA
     VIPGLSTEQQ PSAQELAALA GQMREQGVRV ILSENPPGDR LSAALAEEAG AVVAPPIYVG
     ALGAPGSGSD TYLGAMRYNI DTIADALTTA RKPQP
//
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