ID A0A1X7DYN2_9ACTN Unreviewed; 604 AA.
AC A0A1X7DYN2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycine betaine/proline transport system substrate-binding protein {ECO:0000313|EMBL:SMF23618.1};
GN ORFNames=SAMN02745830_02391 {ECO:0000313|EMBL:SMF23618.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF23618.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF23618.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF23618.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the OsmX family.
CC {ECO:0000256|ARBA:ARBA00035642}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the binding-protein-
CC dependent transport system permease family.
CC {ECO:0000256|ARBA:ARBA00035652}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWZW01000004; SMF23618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7DYN2; -.
DR OrthoDB; 9787902at2; -.
DR Proteomes; UP000192930; Unassembled WGS sequence.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd13639; PBP2_OpuAC_like; 1.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR47737; GLYCINE BETAINE/PROLINE BETAINE TRANSPORT SYSTEM PERMEASE PROTEIN PROW; 1.
DR PANTHER; PTHR47737:SF1; GLYCINE BETAINE_PROLINE BETAINE TRANSPORT SYSTEM PERMEASE PROTEIN PROW; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF04069; OpuAC; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Reference proteome {ECO:0000313|Proteomes:UP000192930};
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 49..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 90..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 133..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 201..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 239..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 87..266
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 604 AA; 64513 MW; 549C1F3F07FF99C8 CRC64;
MPRFHLGDHV DSGVDWLVTH LSWLFDAVKT VVEGLYDGLD AVLTAPEPLL LAGILAVLAW
WLRGLAAGVL AFAGFALIDS LALWDEAMST LSLVLVATLI ALVISVPLGI WAARSKAVAA
TLRPVLDLLQ TMPSMVLLIP AILFFGMGVP AGVVATLIFA LAPGVRMTEL GIRQVDAELV
EAAEAFGTRP RDTLLRVQLP LALPTIMAGV NQVIMLGLSM VVIAGMVGTG GLGGAVNEAI
GRLDIGLGFE AGLGIVVLAI YLDRMTGALG TRISPLGRRA AARARTTMWT YRPRAAVAVV
GVVVLALAAG GLGLTGSKGG PADTSATNVG RGEEITIGYI PWDEGIASTY LWKELLERRG
FEVTATQYTA GPLYTGLATG RIDFQTDAWL PTTHAEYWKK YGDQLADLGK WYGPTSLELT
VPAYMKDVNT LADLKAHASE FGGRITGIEP SAGMMGLLKD EVLPRYGLED AYEVVDGSTP
AMLAELKRAY AKKQPIAVTL WSPHWAYSQY DLKKLKDPEG AWGEGDGVHT VARKDLAADQ
PEIGAWLKDF SMTEEQLTGL EARIQQAGKG REQDAVRTWL KEHPGLVEKW VPVAESGEKS
GAGR
//