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
//