ID E0S171_BUTPB Unreviewed; 728 AA.
AC E0S171;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Bacteriocin ABC transporter ATP-binding/permease/protease protein {ECO:0000313|EMBL:ADL33546.1};
GN OrderedLocusNames=bpr_I0803 {ECO:0000313|EMBL:ADL33546.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33546.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33546.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001810; ADL33546.1; -; Genomic_DNA.
DR AlphaFoldDB; E0S171; -.
DR STRING; 515622.bpr_I0803; -.
DR MEROPS; C39.005; -.
DR KEGG; bpb:bpr_I0803; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_95_3_9; -.
DR Proteomes; UP000001299; Chromosome 1.
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:ADL33546.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:ADL33546.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001299};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..146
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 177..456
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 494..727
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 728 AA; 81103 MW; E7BB961E4491D4DE CRC64;
MAFMGANRTV KKPSVGKRVH VPIVMQMEAL ECGAACLDMI LAYYGKWIPL EKVRYDCGVS
RDGSNAKNIL CAARNYGLEA SGYRFEPETL VKSGSFPCII HWEFNHFVVL CGFQGGYAYI
NDPGRGILKM PMSEFDEGFT GIVLCFEPGD NFVQSGKKMR TIDYVNIRLK GASKAVIFVL
FSTFVAYLFN TLNPAFSRFF MDRLLSGENK ELLMPFIVLF SAVAFFNIVS SAVSDIYSLR
IDGKLSVLSN SNYVWKVLHL PMNFFSQRLS GDILQRKGSQ ISKILVDTVA PLLLNFVMMI
FYLVFMLRYS PLLSLIGIAS IVLNSFVGRL ISRKRVNITR CSLRDSAKLE STTLSGVMMI
ETIKSSGAEA GFFKKWAGYQ AAVNKEKIEY GHINIWLGSI PALINSLAGY MVLILGVALV
MRDQFTLGMV LSFQMYLSYF TAPAMGIIGA GQSIEEMRSM MERYEDVMQY PDDELFDAES
ISDDQEYQKL KGDIHLRNVT FGYSRLANPV IKDFSLDIAE GSKVAIIGAS GCGKSTLSKL
ISGLYKPWSG EITFSDKTIE QIDRNVFTGS VAVVDQDITL FQDTIDQNIK LWDNSIEDFE
VILAARDAGI HDEIMERDAG YKGAVAENGN NFSGGQKQRL EIARVLAQDP SIIILDEATS
ALDAVTEMKV IEAIKKRGIT CVVIAHRLST IRDCDNIVVL RDGEIAEQGT HEELLEKGTY
YKELVTNE
//
