ID   SYRD_PSESY              Reviewed;         566 AA.
AC   P33951;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=ATP-binding protein SyrD;
GN   Name=syrD;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B301D;
RX   PubMed=8231810; DOI=10.1111/j.1365-2958.1993.tb01738.x;
RA   Quigley N.B., Mo Y.-Y., Gross D.C.;
RT   "SyrD is required for syringomycin production by Pseudomonas syringae
RT   pathovar syringae and is related to a family of ATP-binding secretion
RT   proteins.";
RL   Mol. Microbiol. 9:787-801(1993).
CC   -!- FUNCTION: ATP-driven efflux pump necessary for the secretion of
CC       syringomycin. May specifically bind syringomycin and translocate it to
CC       the periplasmic space. SyrD is also required for full expression of the
CC       syrB gene.
CC   -!- SUBUNIT: Dimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; M97223; AAA16337.1; -; Unassigned_DNA.
DR   PIR; S37347; S37347.
DR   RefSeq; WP_003408051.1; NZ_RBRX01000129.1.
DR   AlphaFoldDB; P33951; -.
DR   SMR; P33951; -.
DR   TCDB; 3.A.1.113.1; the atp-binding cassette (abc) superfamily.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1904680; F:peptide transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:InterPro.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005898; Cyc_pep_transpt.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43553:SF11; PTHR43553:SF11; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR01194; cyc_pep_trnsptr; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..566
FT                   /note="ATP-binding protein SyrD"
FT                   /id="PRO_0000092983"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          22..301
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          343..566
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         380..387
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   566 AA;  63196 MW;  79EAA6267053B922 CRC64;
     MKTKQEKKAR PGSIMRLLWS SHPWLTFFTL LTGLISGVAS IAVVNVINQA IHEETFQRQS
     LFWFVGLSVV ALLFRNGASL FPAYASMRIM TRLRIALCRK ILGTPLEEVD RRGAPNVLTL
     LTSDIPQLNA TLLIMPTILV ESAVFLFGIA YLAYLSWVVF AITISLMILG VAMYLLFFMG
     GMKFTHKVRD EFTAFNEYTH ALVFGLKELK LNGIRRRWFS RSAIQESSVR VAKYNYIERL
     WFTAAENVGQ LTLSLLVGCL LFAAPMFAVI DAKTMSASVL AVLYIMGPLV MLVSAMPMLA
     QGRIACTRLA DFGFSINEPH PEPETSDADN VLLLDHKKSW GSIQLKNVHM NYKDPQSSSG
     FALGPIDLTI HSGELVYIVG GNGCGKSTLA KVFCGLYIPQ EGQLLLDGAA VTDDSRGDYR
     DLFSAVFSDF HLFNRLIGPD EKEHPSTDQA QTYLSTLGLE DKVKIEGLGY STTTALSYGQ
     QKRLALVCAY LEDRPIYLLD EWAADQDPPF KRFFYEELLP DLKRRGKTIL IITHDDQYFQ
     LADRIIKLAD GCIVSDVKCA VEGKRA