ID A0A096AUS1_9BACT Unreviewed; 737 AA.
AC A0A096AUS1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:KGF34327.1};
GN ORFNames=HMPREF2137_08955 {ECO:0000313|EMBL:KGF34327.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF34327.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF34327.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF34327.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF34327.1}.
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DR EMBL; JRNN01000072; KGF34327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A096AUS1; -.
DR MEROPS; C39.001; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000029556; 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; cd18571; ABC_6TM_peptidase_like; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
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:KGF34327.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..134
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 182..461
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 495..731
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 737 AA; 83949 MW; A21779DE899F8C5F CRC64;
MRGWDFSNMQ VVFQHDTMQC GIACLTMICQ HFGKKVSLNF LSKMCCSTSE GTSLLSISET
ASKIGLNAVC YKISLSDLSK IQTPCILHWN QNHFVVLYKI VNNKRFFIAD PAKGRLVCGE
KELETHWTSK EISNNANGIV MYFYPTKKFY LLGNDNSLLE NSHSFKFLFG YINRFSRYFG
QILLGLLLGS LLQLILPFLT QSIVDVGIKN QNIGFIWLIL LGQLMLTVSR TAIDFIRRWL
LLHISLRINI SLVSDFFIKL LRLPMSFFDT KLMGDLMQRM NDHSRVNTFL TQQTLSIVFS
LFTFVVFSIV LPSYNWLVFA IFMLGSLLYG GWLALFLRRR KVLDYELFEQ QAINNNKTYE
FITSMQEIKL QDCEQRRRWE WEDVQADLFG VQMKSLKLQQ TQEAGSIFIN ELKNIVITVV
AATAVIHGQL TLGMMLAVQY IIVQLNSPVE QLMSFFYSVQ DVKISLERIN EIHRMDDENG
KQGLETSVKE ENKGIDLENV NFKYDPHALK AIIDDVSLAI PKGKVTAIVG ASGSGKTTLI
KLMLGYYPVL GGQITIGGTD VNTLNKKWWR RQCGVVMQDG VIFSESIARN IAVDDGEIDK
ERLQRSAEIA CIHDYVMGLP LKYNTKIGRD GVGLSQGQRQ RILIARAVYK NPDYIFLDEA
TNSLDANNER MIVEHLDEFY KGKTVVIVAH RLSTVKNADQ IVVLYKGKVV EIGNHEVLTA
KRGVYYNLVK NQLELGN
//
