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Database: UniProt
Entry: A0A1F8QZX1_9CHLR
LinkDB: A0A1F8QZX1_9CHLR
Original site: A0A1F8QZX1_9CHLR 
ID   A0A1F8QZX1_9CHLR        Unreviewed;      1137 AA.
AC   A0A1F8QZX1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=ABC transmembrane type-1 domain-containing protein {ECO:0000259|PROSITE:PS50928};
GN   ORFNames=A2W36_03240 {ECO:0000313|EMBL:OGO40987.1};
OS   Chloroflexi bacterium RBG_16_58_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797654 {ECO:0000313|EMBL:OGO40987.1, ECO:0000313|Proteomes:UP000180315};
RN   [1] {ECO:0000313|EMBL:OGO40987.1, ECO:0000313|Proteomes:UP000180315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000256|RuleBase:RU363032}.
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:OGO40987.1}.
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DR   EMBL; MGNV01000089; OGO40987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8QZX1; -.
DR   Proteomes; UP000180315; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; MetI-like; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43386; OLIGOPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN APPC; 1.
DR   PANTHER; PTHR43386:SF1; OLIGOPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN APPC; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 4.
DR   SUPFAM; SSF161098; MetI-like; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363032};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363032}; Transport {ECO:0000256|RuleBase:RU363032}.
FT   TRANSMEM        27..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        174..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        237..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363032"
FT   DOMAIN          23..257
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50928"
SQ   SEQUENCE   1137 AA;  123729 MW;  7C179B0B40956F8C CRC64;
     MPGFPLGSDQ FGRNLYSRIL YAIQPTMVMV IIVALMRQFL GTVIGLGAGW SRGRTGRLLD
     TLISGALSVP VFMIALGAIA MLGASGGNLL LLAQALKAPE SLLAVFKATS NSTIDQILPF
     VLGLSINGWG ETARIVREQT QMVRGQLYIE AAHAMGASSG SILKQHVLRQ IMSMVWMLFA
     FEISSTLMVT AGLGFLGYYI GGDVWIEVAD FVSRRVSGTP ELGQMLATSW TTLTEPWPMV
     LIGTVIFLAV LGFNLLGEGL RVRLNPENIN RNSLFARMKR AVSSWTEEYI TYPTSNWLRQ
     HAATAILAGV LLVVLVTGGI WLKSILFAPE DRTGQVAEVP GGQLWSGERG NPYGTRSSPE
     AGPQAPTIVW QFQEAGGLAN GLAISKEGTI YLGSLQKKLM ALNPDGTISW EAGLDEVPMS
     APAVGVDGTI YVTDNSGGLT AFNPQGEQLW YYPPNEQGKP AHGAITAEDG SIYYLLEDAQ
     RGDTLVALAA DGSLRWSTAT GTKAADTALR LSSDGKEIYV KNQALSAENG ELLERSLPTA
     ADPVLSGHEQ YFIGADQQRY LRAGHIVMRW EVKGGDFELL QNTEWNYLTL GYGPNSSFPN
     DAGASQDQKI WLFYSWQYGG TTLIWLEPAG EVIGISSLPL SNNSILASID SQNTAYVCGQ
     EPDTGNQPPP KCMAYRRGSA QPEWEIALEG SMTEVSAAAL AAGRLYVVTK DGFLFVIGQG
     GQVAEMGMGT AEAGQPTDEA TEQTAGVGET PAAAGELLWT YQFPGVVGGG LSEQEDGSLM
     AITIDNELIK IDAQGKVVSQ IMVEPGPYQH PEGRFIIEPI ALSNGSYLVV SSEKSAYAMD
     AAGVKLWEVP LAANPAGMTE RRGDTVYLSD LAGNLYAFGA QGLLWQFKPD GATKATNRPI
     VGPDGRLYFV VLIEHRAYVQ AVNPDGTPSW QAPVKTGFFT YDLQINGAGT LLFLREDIYD
     TQAGMRLELT PPFRVDEYIM GEDGLNYVRT GHVVSQWELT ENGMEIVKTA SWNYQSMGQP
     PFMSFVTAQK VIWLYYGSKL IWLDMDGNVF NTIPLENSSI QRWDEENTRY YACEQPIRSE
     QLTCKMYTVD SNGPVWEMTI TGLPDTQWGW ITEEGLTAIT KENVVYRLKV DWPEPKD
//
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