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Database: UniProt
Entry: A0A1E4JZY0_9PROT
LinkDB: A0A1E4JZY0_9PROT
Original site: A0A1E4JZY0_9PROT 
ID   A0A1E4JZY0_9PROT        Unreviewed;       707 AA.
AC   A0A1E4JZY0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Peptide ABC transporter substrate-binding protein {ECO:0000313|EMBL:ODU32409.1};
GN   ORFNames=ABS93_00315 {ECO:0000313|EMBL:ODU32409.1};
OS   Thiobacillus sp. SCN 62-729.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1660148 {ECO:0000313|EMBL:ODU32409.1, ECO:0000313|Proteomes:UP000094151};
RN   [1] {ECO:0000313|EMBL:ODU32409.1, ECO:0000313|Proteomes:UP000094151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- FUNCTION: Probably part of an ABC transporter complex that could be
CC       involved in peptide import. {ECO:0000256|ARBA:ARBA00037680}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000256|ARBA:ARBA00005695}.
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:ODU32409.1}.
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DR   EMBL; MEFL01000004; ODU32409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4JZY0; -.
DR   Proteomes; UP000094151; Unassembled WGS sequence.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd08505; PBP2_NikA_DppA_OppA_like_18; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290:SF88; OLIGOPEPTIDE-BINDING PROTEIN APPA; 1.
DR   PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 2.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        677..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..577
FT                   /note="Solute-binding protein family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00496"
SQ   SEQUENCE   707 AA;  79573 MW;  BA65D5C47D7833A9 CRC64;
     MVRIGAILLR MGLLGMGVGL LAGCSDSWNN PYPGADAHAN VLYSAFSERP KHLDPARSYS
     SNEAEFTGQI YEPPLQYHFL KRPYTLIPLT AEAVPTPYYL DAAGKPLADD APAAAIAESV
     YEIRIRPGIR YQPHPAFARD AAGHYRYHAL DAAALTGKRQ IGDFTHTGTR ELVAADYVYQ
     IKRLANPRLS SPIFGLMSEH IVGLKALGDT LEKVSRAHPD MELNLNDFPL AGAEVVDRYT
     YRIHIKGKYP QFIYWLAMPF FAPVPWEADA FYAQPGMADN NLLSENDPNR RMVLTKNPYY
     HGETYPEDGD AADRQAGLLA DAGKPLPFVD KAVFSLEKET IPYWSKFLQG YYDSSGINSD
     SFDQAVQFSA GGDPRLTDNM REKGIHLVTA VAASIWYVGF NMLDPVVGGQ GEDRRKLRQA
     ISIAFDYDEF ISIFLNGRGI PAQGPIPPGL FGYVDGVAGL NPYVYETHDG KIVRHSIEMA
     KKLLAEAGYP NGRNVKTGEP LVLYFDTMAS GPDTKSRLDW MKKQLDKLNV QLVVRGTDYN
     RFQDKMRKGN AQLFEWGWNA DYPDPENFFF LLYGPNKKVA TGGENAANYD NPEFNRLFER
     MKDMDNGPER QRVINAMLEI VRRDAPWIFA YYPKSFGLRH DWVHNVKPNL MANNTLKYRR
     IDPDLRAARR AEWNRPVLWP ILLLVGGVVA LIAPAVVAWR RRERTTA
//
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