ID K4R4A5_STRDJ Unreviewed; 858 AA.
AC K4R4A5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:CCK31106.1};
GN ORFNames=BN159_6727 {ECO:0000313|EMBL:CCK31106.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK31106.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK31106.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE971709; CCK31106.1; -; Genomic_DNA.
DR AlphaFoldDB; K4R4A5; -.
DR STRING; 1214101.BN159_6727; -.
DR KEGG; sdv:BN159_6727; -.
DR PATRIC; fig|1214101.3.peg.6815; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1131; Bacteria.
DR eggNOG; COG1716; Bacteria.
DR HOGENOM; CLU_012042_1_1_11; -.
DR OMA; NGYRMPV; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03213; ABCG_EPDR; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.60.200.20; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00498; FHA; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00240; FHA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CCK31106.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 595..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..92
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 200..250
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 282..523
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 103..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 93024 MW; 49697BE170269EFA CRC64;
MFDIPRLPVM GRNSGDYSVG HGVPELVLEL NGQTWTLDPS RTYTLGRDPQ GDIVLDDARV
SWRHATISWS GRSWAIEDHG STNGTFVAGQ RIHQLEIGPG SAVHLGNATD GPRVSLSGSA
ASAAPQPQQQ QPYAAQGANP GWAQQAPPQH QAPQADWQQP QQAAHNIPQQ QGPGVGAGAP
PVYGDRSPTT FHQFAIGRVM RIGRALENEL VVSDLQVSRH HAEFHSTPDG RMEIRDLGSH
NGTYVNGQPI AKGGSQLLGP ADIVGVGHST FRIVGDRLEE FVDTGEVSFS ARHLTVTVDG
GKQILKDVSF GVPEKSLIAV IGPSGSGKST LLKALTGYRP ANQGDVLYDN RNLYKQFAEL
RQRIGLVPQD DILHKELTVK KALKYAAKLR FPADTTAQER EARIDEVLRE LKLDIHKEKK
VTSLSGGQRK RVSVALELLT KPSLIFLDEP TSGLDPGMDR DVMQLLRGLA DDGRTVLVVT
HSVAELAICD KLLVMAPGGA VAYFGPPEEA LNFFGYDSWA DVFSAFENYR DYDWAGRWKG
SQHYQMYAAD IDAIAPQSVQ MPPMQAMRPP KPQGWMSQFG TLVRRYASVI VSDKGFLALS
IILPLVLGSV SLLIDSGKDL LVNTEINPNT GQPVANGTAL TVLLILAVGA CFAGAANSVR
ELIKERVIYE RERATGLSRS AYLMSKVFVL GLITMVQGLM VGIIGFSSRT IPDEGLILGS
QILLELCIPI MALGFTAMMF GLIISALVKT AEKTMPLLVM FAIVQVVFTG CLFPLANSVG
VNELSYLMPS RWAVAAAGAT LDFNKISPPA KGDSNDPLWE HTVGAWGMDM VALIVLGVVC
GFFVARFLRR HEPEVMRK
//