ID   Q11H77_CHESB            Unreviewed;       540 AA.
AC   Q11H77;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Twin-arginine translocation pathway signal {ECO:0000313|EMBL:ABG63248.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Meso_1855 {ECO:0000313|EMBL:ABG63248.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG63248.1};
RN   [1] {ECO:0000313|EMBL:ABG63248.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG63248.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably part of an ABC transporter complex that could be
CC       involved in peptide import. {ECO:0000256|ARBA:ARBA00037680}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000256|ARBA:ARBA00005695}.
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DR   EMBL; CP000390; ABG63248.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11H77; -.
DR   STRING; 266779.Meso_1855; -.
DR   KEGG; mes:Meso_1855; -.
DR   eggNOG; COG0747; Bacteria.
DR   HOGENOM; CLU_017028_7_2_5; -.
DR   OrthoDB; 9803988at2; -.
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; cd08512; PBP2_NikA_DppA_OppA_like_7; 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; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   InterPro; IPR006311; TAT_signal.
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; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          78..449
FT                   /note="Solute-binding protein family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00496"
SQ   SEQUENCE   540 AA;  59377 MW;  A6CD3D0BE16A6B18 CRC64;
     MSNFMLTRRQ LLAGTASAGI TFGVGPTMPF AAAADKRTLR LADGNIGQAD PHKPVDFPGS
     ILMFNLYDFL VRPAPGGEIE PSVAESWEIS EDGKVYAFTI RDGIKFHDGS PLTAEDVVFS
     ANRMITMKRG FSFLLAAVEK AEQDGNKVIF RLREPFSPFL AALVRLAIVN KKLVTANLKD
     GEFGEFGDYG EAFLSSNDAG SGPYKIARHD SQNETVMEIN PDYFAGFAPN PPEVVRSKFG
     VEAVTVRQLM PRGEIDLTRL PLPPEIVAAL SQSDGISIGQ DRKPTIFHFK MNTQKAPLDD
     VNVRKAIALA FDYDQLYALL DVAGQQQGTP IRGPIPADVM GYDPGVPLIK RDIEAAKAAL
     AESKYADQPL ELNLVWFKSV ALQEKFALLL QANLAELGMK VNITSAPWPQ IVEMATSPEA
     TPHLACVATS LSTTDVDSML WAEYHSSAAG TYLSMHWLQK PEIDAALEKG RQTTDPAARH
     ELYKELARVI ADEYPSVFLY QAIDLVAFRE NLHVPGFEDP KQSIPIMAGN YRYDRMTMDV
//