ID A0A1A9C0H4_9ACTN Unreviewed; 782 AA.
AC A0A1A9C0H4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein {ECO:0000313|EMBL:SBT93715.1};
GN ORFNames=GA0115233_106941 {ECO:0000313|EMBL:SBT93715.1};
OS Streptomyces sp. DI166.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT93715.1, ECO:0000313|Proteomes:UP000198690};
RN [1] {ECO:0000313|Proteomes:UP000198690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FLSP01000069; SBT93715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9C0H4; -.
DR STRING; 1839783.GA0115233_106941; -.
DR OrthoDB; 9806127at2; -.
DR Proteomes; UP000198690; Unassembled WGS sequence.
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 GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd18569; ABC_6TM_NHLM_bacteriocin; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR022514; NHPM_micro_ABC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR03796; NHLM_micro_ABC1; 1.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SBT93715.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198690};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..188
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 220..500
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 540..773
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..54
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 84017 MW; 5A96E471F64C499D CRC64;
MSDTKSTTAT RTTGPGGPPG GPGRDAPVSR RRTRRAERRG RRGAARERRW ARRRAHRVPT
VLQMESVECG AASLAMILAH HGRHVPLEEL RSLCGVSRDG AKASSVLAAA RSFGMVARGF
QAEPDLLREK LRTGPVIIFW AFQHFMVVEG ISTRFGRTLV AVNDPSTGPR LMEWSEFDSG
FTGIVLTFEP GPDFRPGGRR TSTAAALLDR RLPSGRALPL VLLASLLLVV PGIVGAAYSR
VFVDQVIGAD SPTAVLPLAL AMAVTALMVF VLTSVQQHYL LRMEIRTGLV SSARFFRHLL
RLPIEFFLQR RPAEVAKRVA SNDTVAMILS RDVAATTINL TLVVFYGALM IRYDVLLGAI
GLATAGLNVL MLQLVARSRK DAVAALRADR GNLIGTTFAT LSTIESVKAS GSEPEAFTRW
AGFLAKVTSA QQRLGQTTAV LTVLPPLLAV VNIGVLLLVG GLRVADGTLS VGILVTFQTL
LAALSRPVTQ LTNLGSRLQD MNADLKRIHD VEKYPQAGCF EPGRDELDPE APEGRLNGEL
VLRDITFGYG PLAAPVISGL CLTITPGSRT AVVGGSGSGK STVGRLVTGL YEPRSGQVLL
GGRPREEIPR TVLAASMAYV DQDVALFSGT VRENLTLWDD TVPDEVVLAA LQDAAVFDEV
LSRPGGLNAQ VWEHGANFSG GQRQRLELAR ALAARPTLLV LDEATSALDP ATERTVMDNL
RRRGCACLII AHRLSTVRDA DEIIVLDKGT VAERGTHDEL LAARGLYAAL FESSRAEESD
TL
//
