ID A0A0U3PT41_9ACTN Unreviewed; 682 AA.
AC A0A0U3PT41;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=ABC transporter {ECO:0000313|EMBL:ALV35794.1};
GN ORFNames=AS200_29930 {ECO:0000313|EMBL:ALV35794.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV35794.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV35794.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV35794.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC {ECO:0000256|ARBA:ARBA00005417}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
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DR EMBL; CP013743; ALV35794.1; -; Genomic_DNA.
DR RefSeq; WP_058925397.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PT41; -.
DR STRING; 1725411.AS200_29930; -.
DR KEGG; scx:AS200_29930; -.
DR OrthoDB; 3677453at2; -.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015833; P:peptide transport; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd03257; ABC_NikE_OppD_transporters; 1.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01727; oligo_HPY; 1.
DR PANTHER; PTHR43297:SF6; DIPEPTIDE TRANSPORT ATP-BINDING PROTEIN DPPD; 1.
DR PANTHER; PTHR43297; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 91..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 137..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 89..279
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
FT DOMAIN 365..606
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 71026 MW; 5C92C1D7DACD3D72 CRC64;
MFTRARLTEV LARPGIRLRG PRRLPPPSRA AVCFLALVVL VAVLAPLIAP DDPLDQQEPA
GGTGHPSAAH WMGQDSLGRD ILSRLMYGAR WSLAIGLGAT ALALVVGALI GAVAATSRKA
VDETLMRCLD IVMAFPGIAL AAVLVAVFGG GITVLICAIA FLFTPPVARV VRANVLDQYG
EDYVTAERVI GARTPHIVLR HVTVNCAAPV LVFCTVQVAE AIVFEASLSF IGAGVRPPDP
SWGSVIADGK NMVLTGGWWA TVFPGLLMLV TVLSLNILSE GVSDAWASPA GREVGSAADE
DRVEAPDAGG GEVLHLPGLA EAAARLRGRG RGRGAGGGAT GGGSAGAAAG GLVAQFPAPL
QGAVLSVESL VIGFEGRHSG VDIVDGVSFE VRPGEVLGLV GESGCGKSLT ALTVMGLQPR
GARVGGHVRF QGRELLTLSP RARRRLLGHE MAMIYQDALS SLNPAMTVRA QLKQVVRRGG
RRTPEELLTM VGLDPARTLR SYPHELSGGQ RQRVLIAMAL SRDPKLIVAD EPTTALDVTV
QAQVMELLLR LRGELGFALV LVSHDLALVA DITDRVAVMY GGQIVETGVT ADLVEAPAHH
YTRGLLGSVL SLESAAARMT QIRGVVPSPA DFPAGCRFAD RCPLATDVCR TTAPALLGTP
THTAACHHPA VALAASEPEA VQ
//
