ATNG_EMENI
ID ATNG_EMENI Reviewed; 1557 AA.
AC Q5AV01; A0A1U8QZH1; C8V3Y4;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ABC transporter atnG {ECO:0000303|PubMed:26563584};
DE AltName: Full=Aspercryptin biosynthesis cluster protein G {ECO:0000303|PubMed:26563584};
GN Name=atnG {ECO:0000303|PubMed:26563584}; ORFNames=ANIA_07879;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION OF THE CLUSTER.
RX PubMed=23248299; DOI=10.1073/pnas.1205532110;
RA Andersen M.R., Nielsen J.B., Klitgaard A., Petersen L.M., Zachariasen M.,
RA Hansen T.J., Blicher L.H., Gotfredsen C.H., Larsen T.O., Nielsen K.F.,
RA Mortensen U.H.;
RT "Accurate prediction of secondary metabolite gene clusters in filamentous
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E99-E107(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=27310134; DOI=10.1021/acschembio.6b00398;
RA Henke M.T., Soukup A.A., Goering A.W., McClure R.A., Thomson R.J.,
RA Keller N.P., Kelleher N.L.;
RT "New aspercryptins, lipopeptide natural products, revealed by HDAC
RT inhibition in Aspergillus nidulans.";
RL ACS Chem. Biol. 11:2117-2123(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26563584; DOI=10.1002/anie.201507097;
RA Chiang Y.M., Ahuja M., Oakley C.E., Entwistle R., Asokan A., Zutz C.,
RA Wang C.C., Oakley B.R.;
RT "Development of genetic dereplication strains in Aspergillus nidulans
RT results in the discovery of aspercryptin.";
RL Angew. Chem. Int. Ed. 55:1662-1665(2016).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of aspercryptins, linear lipopeptides built from six amino
CC acids including 2 highly unusual and nonproteogenic amino acids, 2-
CC amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol)
CC (PubMed:23248299, PubMed:27310134, PubMed:26563584).
CC {ECO:0000269|PubMed:23248299, ECO:0000269|PubMed:26563584,
CC ECO:0000269|PubMed:27310134}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the aspercryptin
CC cluser-specific transcription factor atnN (PubMed:27310134).
CC {ECO:0000269|PubMed:27310134}.
CC -!- DISRUPTION PHENOTYPE: Does not alter the yield of aspercryptin
CC significantly (PubMed:26563584). {ECO:0000269|PubMed:26563584}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; BN001302; CBF73441.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59533.1; -; Genomic_DNA.
DR RefSeq; XP_681148.1; XM_676056.1.
DR AlphaFoldDB; Q5AV01; -.
DR SMR; Q5AV01; -.
DR STRING; 162425.CADANIAP00003895; -.
DR EnsemblFungi; CBF73441; CBF73441; ANIA_07879.
DR EnsemblFungi; EAA59533; EAA59533; AN7879.2.
DR GeneID; 2869038; -.
DR KEGG; ani:AN7879.2; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_5_1; -.
DR InParanoid; Q5AV01; -.
DR OMA; FTWINPL; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 1.
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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1557
FT /note="ABC transporter atnG"
FT /id="PRO_0000444136"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1020..1040
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 279..556
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 593..829
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 882..1162
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1199..1431
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1439..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 625..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1233..1240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1557 AA; 173274 MW; 1EB7747106957C5A CRC64;
MAGSCTIDEH NHFGPIVGDA CYGGLDFTLY FEEAFLSIFP AATLILAATV RCFLVRSASL
KVRGGWLHTL KLLLLAPYSI SQLLLLAFWM RSGTPKTDLT IASTVLRFIA TLPCGYLIHL
QHHRSLRPSK IISIYFLLTL LFDIPLARTI WTIQGLRTVS AIFIAGTVVK ALLLILETWE
KRRLVRPMYA SPAPEDWTGV INRSLFWWIN PLLFRGARTS LSVGDLFHLE SCMLPDPDGK
HRVVMHWENV TNKDKAGAMV VPIAKAFKWD LLAGVFPRLC QSGFIISQPF LVRATVELFV
YRDRPDSRSK ATLLIGAYAL VYGGIAIATA TAQHKTYRVI TMMRAALVDM IFEKSTAINA
HKNDDSAALT LMSTDIERIT HCGRYIHDTW ASLIEIGIAL YLLYNELDTA GIAPIIIAFG
CTVTAMKIAM MAGERQNLWI EAIQKRVAIT AEMLGSMKGV KISGLTDLLF NKIQALREHE
ILASQKFRSL LIAVVGLSNF NTLMTPIVSF TIYAMGSGDA PNEILGSARA LTSLTLFNLF
AVFIGTLVES ISETAMALEC LDRIRNYLAQ EAHQDPREVN SSPVTEKTPC IEAFEVDVGW
KNGDESILHR LSYRIERHSL TMIVGAVGCG KTTLVKAMLG EVNCLTGKMK VNCDRMAYCG
QDAWLTNGSI RENILGGSPY DPPWYSTVVA ACGLEKDFTE LTAGDQTAVG SKGVSLSGGQ
KQRLGSLDVL TRAQALARAL YSGVETILLD DALSGLDPVT DEHIFTQVLG PNGLARKQHL
TVVMVTHAVH RLPYADHIIA LNTDGTILVQ GTFDDCCKRL DYIQGFAIAQ PPAIQMKSAM
PKAVEVTKAA PYSDEAISDA RRSSDYQTYL YYLTTVPWHN WLVYFGLMAI FVFLQAFPTV
WVTWWARDND AQPNKNRSMR IGVYWMFGVL GACFLLATAC FYMLKIVAKT ASVIHSRLLR
TVVNAPMSFF ASTDSGTTLN RFSQDLELID MELPLAVLQT CLALFLCVAQ LIIIAVSARY
ITATIPLCVL VYCIIGTFYM RTSRQLRIME IEAKSPLFSN FMELLNGLIT IRAFNWAEQY
KLRNRALLAE SQRPYYLLYA VQRWLSLVLD MTVAGFVLVL MGIAVGTMHS TNASSLGLAL
VNVVSLSASV KALITDWTVL ETSLGAVTRV KHFAESTESE DMVQERDLPP EDWTSRGTVE
YKNVSAFYRD PSKPVLKNLS FRVHKGEKVA IVGRSGSGKS TLVSALFRMI ELCEGTISVD
GIDITTLRRQ AIRSAIIGLP QDPLLLEGST IRENVDPFDY CPDEAVINTL KRVGLWEILE
SKDGLETIAS PELFSHGQKQ LLCMAKAMLR HGNIIVFDEA TSGVDPETDE MMQELIRSCF
AQHTVLTVTH RLDTIIDYDR VLVMDNGILL ESDPPRTLLS RPSVFRELYK SSRGWEEYER
QERAEAEARR RERVEKERAE EELRGRRGLI SEKEEPETVS AIREHWNVVN QLFGGIIPRA
VPRTRSRSRD HSAERRESKR YSGGDWTGEG DGDGGDGGLG RRDTRRHLTG LAARGLH
