ID A0A1H1X439_9MICO Unreviewed; 1283 AA.
AC A0A1H1X439;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=AcrB/AcrD/AcrF family protein {ECO:0000313|EMBL:SDT03942.1};
GN ORFNames=SAMN04489752_3185 {ECO:0000313|EMBL:SDT03942.1};
OS Brevibacterium siliguriense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1136497 {ECO:0000313|EMBL:SDT03942.1, ECO:0000313|Proteomes:UP000199597};
RN [1] {ECO:0000313|Proteomes:UP000199597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23676 {ECO:0000313|Proteomes:UP000199597};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT629766; SDT03942.1; -; Genomic_DNA.
DR STRING; 1136497.SAMN04489752_3185; -.
DR Proteomes; UP000199597; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2.
DR Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 2.
DR Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 4.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR32063; -; 1.
DR PANTHER; PTHR32063:SF0; SWARMING MOTILITY PROTEIN SWRC; 1.
DR Pfam; PF00873; ACR_tran; 3.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50156; SSD; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1076
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1097..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1129..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..485
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 133029 MW; F8DBA264C64C6A0F CRC64;
MSFLTRLSLQ NRALIALISV VAIIFGVIGA GALKQELFPS LDNPQATVTA SYEGATPEAV
ESEVTDPLEG ALTALPEVED MTSTSSAGSS QITVSTKYGD DSDDVVKALQ RAVSQVQPSL
PDGVEPNVMM MGTDDIPVLA LSVTSDADEE QLAANLEDLV VPELKKVDGV SQVQIAGAKT
KQVEISIRRD DLEDEGANLD EVAGILQSNG VPTSAGELKG TDGTAPVEVG TRIRSIDAIK
GLVISGKDGP IKVSDVADVK LVDEPVESIS RTNGQPSLSV SVMKESDANT VDVSHAVADK
LPELEKMMGD NAEFVSAFDQ APFIEQSIHD LLNEGGLGLI FAVLVILVFL LSVRATIITA
ISIPLSLLIA MIGLWMGGET LNMLTLGALT ISVGRVVDDS IVVIEAIRRR HASGGDKFSN
ILAAVSEVAG AITASTLTTV AVFLPLAFVT GQTGEMFRPF ALTATIALLS SLFVALTIVP
VLAYWFLRQR EAKVKLTRAE KAEIRRSRKS MQAQWRAEKK VAKKADKKRD LVAAGAEAED
IGLRDSGEST RQSVPTGIAV GSPRYGESED GTEEVDELAG MHSPVTRLQK TYMPVIGFST
KHPIVMILVA VLVLAGTGAM IPQLKTELFG DTGQDSLQIS QTFAPGTDLD EASEQAKKVE
DILADASDID NYQLSLGGTT FGFTDDSSLT GTYIVNTKSG VSAQSISADL QKQFDDLDGA
GDVEVASQSS TPGAQTIDVT LTATDAQELE DATNKVSDKL EGVSTAQSVT SDIAAVQPVI
EVKVDHEKAA EENLTEASIG QYVQRAMHGQ QIGEVVIDDV SHSVLLFDRN ADTVEKLREL
KIPGKPEQTA PAGGAGAGAA GGAGGSGDAG VAGGAGGGPG GSGDAGGAGG AGGGAGGAGA
AGGAAGGDPN AGAPVTAEPR FIELDDVADV KEVKTAPTIR HTDSQRSTTV SVTPEGDDLG
AVSTEVQSAL DEVDLPDTVS VDTGGATQEQ NEAFSQLGLA MLAAILIVFV IMVATFKSLL
QPLILLVSIP FAATGSVALS LITDTPLGLT SMIGLLMLIG IVVTNAIVLI DLINHFRVRG
VDLRTSIVHG ARLRYRPILM TAAATIFALL PMALGLTGGG VFISKPLAIV VIGGLVSSTL
LTLILVPVLY LLLEGVKERR AEKKHVKNMA RGEVLDAAEA RSSQRETATV PAGAGAGAGD
LRTQTEGEAS TEAAAPTADS TSADSGRTAS AWDEAAPADR VDDGLTVNDG RDADADRGDA
AETDFTLRSQ NPRRDDGNGE PKH
//
