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Database: UniProt
Entry: A0A0T1SIN8_9ACTN
LinkDB: A0A0T1SIN8_9ACTN
Original site: A0A0T1SIN8_9ACTN 
ID   A0A0T1SIN8_9ACTN        Unreviewed;       271 AA.
AC   A0A0T1SIN8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
GN   ORFNames=ASD33_10600 {ECO:0000313|EMBL:KQX53593.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX53593.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX53593.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX53593.1,
RC   ECO:0000313|Proteomes:UP000051136};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363076};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363076}.
CC   -!- SIMILARITY: Belongs to the SURF1 family.
CC       {ECO:0000256|ARBA:ARBA00007165, ECO:0000256|RuleBase:RU363076}.
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:KQX53593.1}.
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DR   EMBL; LMEP01000012; KQX53593.1; -; Genomic_DNA.
DR   RefSeq; WP_056561220.1; NZ_LMEP01000012.1.
DR   AlphaFoldDB; A0A0T1SIN8; -.
DR   STRING; 1736450.ASD33_10600; -.
DR   Proteomes; UP000051136; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd06662; SURF1; 1.
DR   InterPro; IPR002994; Surf1/Shy1.
DR   InterPro; IPR045214; Surf1/Surf4.
DR   PANTHER; PTHR23427; SURFEIT LOCUS PROTEIN; 1.
DR   PANTHER; PTHR23427:SF2; SURFEIT LOCUS PROTEIN 1; 1.
DR   Pfam; PF02104; SURF1; 1.
DR   PROSITE; PS50895; SURF1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU363076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363076};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363076};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363076}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363076"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363076"
FT   REGION          244..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  29770 MW;  5102EDCF52AD4C11 CRC64;
     MYRFLLSRQW VILTLVALVL IPTMIELGFW QFHRHERRVA QNTLIADSVA AKPVPVEELT
     SPGHTVPRED YWRPVTATGT FDTAHEVVVR RRTSSDDRVG VHVLTPLVLR DGAVVLVNRG
     WIPAAADQHS FPPVPPAPKG EVTVTGRLKA DETTGASGIK DLKGLPDRQV MLISSRQQAE
     LIGREVLGGY VEQVTPAPAG DTPEPIAEPD HDSIGPHMAY AVQWWLFAGG VPVGWVILVR
     REKRDRETAA ASDTTVTPER DTEAIQATPS P
//
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