ID   A0A1W9SR22_9BACT        Unreviewed;      1503 AA.
AC   A0A1W9SR22;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Solute-binding protein family 3/N-terminal domain-containing protein {ECO:0000259|SMART:SM00062};
DE   Flags: Fragment;
GN   ORFNames=B6I20_10670 {ECO:0000313|EMBL:OQX98790.1};
OS   Bacteroidetes bacterium 4572_117.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1971632 {ECO:0000313|EMBL:OQX98790.1, ECO:0000313|Proteomes:UP000192701};
RN   [1] {ECO:0000313|Proteomes:UP000192701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQX98790.1}.
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DR   EMBL; NBLH01000175; OQX98790.1; -; Genomic_DNA.
DR   Proteomes; UP000192701; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR35936:SF19; ABC TRANSPORTER ARGININE-BINDING PROTEIN ARTJ-RELATED; 1.
DR   PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR   Pfam; PF07494; Reg_prop; 1.
DR   Pfam; PF00497; SBP_bac_3; 2.
DR   Pfam; PF07228; SpoIIE; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   SMART; SM00062; PBPb; 2.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1503
FT                   /note="Solute-binding protein family 3/N-terminal domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012009680"
FT   TRANSMEM        1232..1250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..270
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   DOMAIN          302..520
FT                   /note="Solute-binding protein family 3/N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00062"
FT   COILED          1279..1320
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1503
FT                   /evidence="ECO:0000313|EMBL:OQX98790.1"
SQ   SEQUENCE   1503 AA;  172622 MW;  11C4B83EF13BB5ED CRC64;
     MNIKTNIKFE INKFILFALL LLFSNQLAVS QSLQQIKENG KIRVAFTESG LRSVNQKFAL
     EFAKFLNVKM EVVPVKWDET FSNNGVILEN YQTTAKINYV PDALRKADLI CGTIYLYEWR
     KKFFDYAGIL ELSDLLIVPS TSKSLKSYEE LDGFTIAILE KSSYETHIEA INDRIGGGIN
     IVKTKSEQQS INLLKNGEVD GYITIAYNAL ETIKESTDFK IAFPVAPIKK AGWAVKKGNT
     ELEEEINNFF ETIKGNGRLN DLFTAHYDMD YNTYYEIISS YSQMQGGKSN QRDLDEIIES
     GKLVVALRDR LMVYNKNNKQ FNTYLAEEFA KYLNVELEVR ITPYFSKYFE NANGEILKDS
     SYTPEWFNNF DVACEIIVPL EWRKKKVNLI PFIPYAQVVI GRKNLNINTL NDLRSFKGVT
     SKGSAQEDIL INNNINNYYY SESNNFLDDI NSGKADYAIG SDAVFRINEF SELEAKFVIG
     QVGKDGWAIK KNQPKLRRKI LEFLDSAKRV GILDKYFRLQ TGMKFKSTEN YLTVLQETYQ
     PGVFPFVFYG TKEGLPQEDI LTIFQDKDNY MWFGTHAGAV KYNGREMKVI DKNNGFNSNS
     IFDIAQDKDG TMFFSTLDGV SIFKDDKVTN IFKGYSFRKV YIDFENNKWF FGDRGIAKYS
     ADGKKRILNK ENLNLPEKVY SITMSKKGIT YIASKQGFFS LNNQFKVHQI SNAPCYSVFI
     DEDKQMWLST INGIYVINIK GYNNQGIGKK INQQLNIPDN TLVKSISQTK DGAVWFVSDD
     KIYQLITLQQ KPIIYDEKVG LEQQRILSFA KDKEENIWIG YAGGIQKLTN KSLRLLYPDK
     VNSYISSIIE DRKGRIWLSM NKNVYVLKDK LENFTKTFNV NEKSYVIGKL PNGNIIIANN
     MALYEIDVEN LKIINRNIFQ KPLQHLENIF ISSQGEIFLL TGIIGNIYYL KNFKSEPVTL
     SNNATSLVSQ LVEYDDMIVG GNKTGLVYFT GKDFDKLQDI GDIVWSLCPD DDILWVGTDN
     GLGKYEDDEY ENVKVNLPNN VINAIKKEND INHLWLGTNG GFAYFNKNTN KVELSIDSKD
     GLQGNEITID GLFIDKRGLL WVGSYHGIST FDIKKNKEIK YSPEGRIERV TLNGKEIAID
     YLLKGLKSNE NNLSFELTGL SFKDEKSIEY EFFMKGLEND YTASRGKNHI AHYTNLPSGK
     YVFNYRTKGN DGIWSYYKQV EFKIEKPIWE EWWFIISVII TMVLLIFGFV KWRNMALQKQ
     NEELERIVKA RTVEILEKNE ELYQQKEEIL AQRDEIVKQK DEAEAQRDEI IQQKKEITDS
     ILYASRIQTA ILPPKAAISK AFPKHFVLYL PRDIVSGDYY WMHQKGDRAI LVAADCTGHG
     VPGAFMSMLG TAFLGQIIGK EKDIPNANII LDQLRYQVIS SLHQTGRENE TKDGMDIAIC
     IIDYDKSVIE YAGAFNSLYQ FRNNELIEHK ADRMPIGVSF NQDKPFSKHV IEFKNGDSFY
     IFS
//