SIRA_LEPMC
ID SIRA_LEPMC Reviewed; 1263 AA.
AC Q6Q876;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Multidrug resistance protein sirA {ECO:0000305|PubMed:15707846};
DE EC=7.6.2.2 {ECO:0000305|PubMed:15707846};
DE AltName: Full=ABC transporter protein 4 {ECO:0000303|PubMed:14749893};
DE AltName: Full=Sirodesmin biosynthesis protein A {ECO:0000303|PubMed:15387811};
DE AltName: Full=Sirodesmin transporter sirA {ECO:0000303|PubMed:15387811};
GN Name=sirA {ECO:0000303|PubMed:15387811};
GN Synonyms=ABCt4 {ECO:0000303|PubMed:14749893};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14749893; DOI=10.1007/s00294-004-0488-6;
RA Gardiner D.M., Howlett B.J.;
RT "Negative selection using thymidine kinase increases the efficiency of
RT recovery of transformants with targeted genes in the filamentous fungus
RT Leptosphaeria maculans.";
RL Curr. Genet. 45:249-255(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=15387811; DOI=10.1111/j.1365-2958.2004.04215.x;
RA Gardiner D.M., Cozijnsen A.J., Wilson L.M., Pedras M.S., Howlett B.J.;
RT "The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus
RT Leptosphaeria maculans.";
RL Mol. Microbiol. 53:1307-1318(2004).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15707846; DOI=10.1016/j.fgb.2004.12.001;
RA Gardiner D.M., Jarvis R.S., Howlett B.J.;
RT "The ABC transporter gene in the sirodesmin biosynthetic gene cluster of
RT Leptosphaeria maculans is not essential for sirodesmin production but
RT facilitates self-protection.";
RL Fungal Genet. Biol. 42:257-263(2005).
RN [4]
RP INDUCTION.
RX PubMed=20507539; DOI=10.1111/j.1364-3703.2007.00433.x;
RA Elliott C.E., Gardiner D.M., Thomas G., Cozijnsen A., Van de Wouw A.,
RA Howlett B.J.;
RT "Production of the toxin sirodesmin PL by Leptosphaeria maculans during
RT infection of Brassica napus.";
RL Mol. Plant Pathol. 8:791-802(2007).
CC -!- FUNCTION: Sirodesmin transporter that provides the dual role of
CC sirodesmin export and self-protection (PubMed:15387811,
CC PubMed:15707846). Provides also tolerance to gliotoxin
CC (PubMed:15707846). {ECO:0000269|PubMed:15707846,
CC ECO:0000305|PubMed:15387811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000305|PubMed:15707846};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is regulated by sirodesmin (PubMed:15707846).
CC Expression is co-regulated with the other genes from the sirodesmin
CC cluster and corresponds with sirodesmin production (PubMed:15387811).
CC {ECO:0000269|PubMed:15387811, ECO:0000269|PubMed:15707846}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased expression of sirP and
CC subsequent production of sirodesmin, as well as to a higher ratio of
CC deacetyl sirodesmin (PubMed:15707846). {ECO:0000269|PubMed:15707846}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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; AY437642; AAR11078.1; -; Genomic_DNA.
DR EMBL; AY553235; AAS92552.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q876; -.
DR SMR; Q6Q876; -.
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:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 2.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Translocase; Transmembrane; Transmembrane helix; Transport;
KW Virulence.
FT CHAIN 1..1263
FT /note="Multidrug resistance protein sirA"
FT /id="PRO_0000437734"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 817..839
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 843..865
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 57..347
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 380..625
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 699..986
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1021..1259
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1056..1063
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1263 AA; 137141 MW; 9AA8F99CD78D3643 CRC64;
MAEPESEKPS SAQGGGLPSS DHPLNPILQR QIELPEIKIN YFSLFRYATV KEYALLLISA
FFAAVSGAMF PLLILFIGNL VQVLKDFNLG TIPQEQLSEQ IRDIALYIVY LFLGQLVSVF
IFTNGCLLVG EAITNAIREK YVRSLFRQNI AFFDTYGSGK ITSQLTSSTA TIQDAISHKI
GLFVSACSCF VASYAIGFVK HWKLTFILTS TVVAITGVMI IMSGFMAKFG ANSSGALAEA
SAKLEETFSG IRVVKALGLE KRLSDELDPQ LLNIEFWGKR VRHVMGWMLA IMYGLIFLNY
GLAIWQGYRF MQGGTEDVGA IITVLMCLNI GAFLFGNVGP HLQAMSLGAA AAQDIFAVIE
RESVTDGGAP PGSFEVEGNI EFRNVSHVYP SRPDTHVLQD FSMIFPAGKV TAIVGASGSG
KSTIVSILER FYEPVSGQVF LDGHDITHLN VQWLRQQFGL VGQEPVLFNG SIFKNVAYGL
KGTQYGQESR EVTMKLVTEA CRIANAHDFI TALPHGYDQE VGIRGASLSG GQRQRIAIAR
AIVSGPKILL LDEATSALDV QSEEAVQLGL NMASSGRTTI VVAHSLSTIK LADNIIVMEK
GRVAQQGTHA ELEAQEGLYQ TFVRRQQLKQ ATLEPPHARI TPAVDTPASP QHRLSEKTGS
IYGQGESEAA DKSPSTKYSF VQLVKFVARF NKEDWRLMVT GIASAVISGA VWPAHSVFFA
KAIVALSSPS PASLARGPNF WAAMYVMLAF VQIASQGVQG SAFAICAERL ILRARRVAFK
YLLRQDVEFF DDPLHSSGIM TSFVSSDVNA LAGLSGVFLG TLFSATATVL GGLILSLAVG
WKLTLVTMGT IPIIIVAGYV RLKLVGTLEK ISRKVHEESA GRVCEEINAV RTVAASCLED
EMCEDYVRSL KSKEKTYLRA TLWSSGWYAL SEAVPLGCMS LGFWYGATLV MRTEYTTEQF
FIVVTAVIFG ASSAGLVFAF APDFGKAGVS AERLQELVDR QPEVDTWSEE GDHIETTNGK
VDVSNVVFYY NQRSKTPVLN SISLGAAPGQ SIGLCGGSGS GKSTVASLLE RFYNPSSGTV
SLDEKDVRTI NINSYRAQFA LVNQEPLLFS CSIRENLLYG SLGKDLTDSE IEEACKMAQV
YDFVCSLPEG LDTSFGSNAV MLSGGQRQRL SIARAILRKP RVLILDEATS ALDSTSERAV
IEALTKTAEG RTTIMVAHRL STIQGCDKIF YLRAGAVAEE GTHEELMAKR GSYYDSVNLQ
SLG
