ID A0A1Y4HWC2_9BACT Unreviewed; 738 AA.
AC A0A1Y4HWC2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:OUP08852.1};
GN ORFNames=B5F34_08310 {ECO:0000313|EMBL:OUP08852.1};
OS Mediterranea sp. An20.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Mediterranea.
OX NCBI_TaxID=1965586 {ECO:0000313|EMBL:OUP08852.1, ECO:0000313|Proteomes:UP000196631};
RN [1] {ECO:0000313|Proteomes:UP000196631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An20 {ECO:0000313|Proteomes:UP000196631};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP08852.1}.
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DR EMBL; NFJV01000011; OUP08852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4HWC2; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000196631; 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 CDD; cd02418; Peptidase_C39B; 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:OUP08852.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000196631};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..136
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 183..462
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 496..732
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 738 AA; 83915 MW; D6B7DDB3E3884855 CRC64;
MAFKQKFPHY RQLDSMDCGP TCLRMIARYY GKSYSLQTLR ERSFITREGV SMLGISDAAE
SIGFRTMGVR ITLKQLQEDM PLPCILHWNQ NHFVVCYDIC RTRKGRIYRI ADPASQLVDY
TETEFGKCWL ATRVGGEEKG AALALVPEPA FYEQEGEAEE GRQRGLRFFF KYLSPYRQQL
VQLVLSMLAV SLLQLIFPFL TQSLVDVGIR DGNLGFITLV LIAQLTVSVS QIAVEFIRSW
ILLHVNTRIN IALISDFLSK LMKLPLRFFD TKMVGDIMQR IGDHNRIEAF LTGSSINTLF
SFVNFFIFGG ILAYYDWRIL LLFVAGNSLY ILWVVGFMKY RRELDIRRFA QAAGEQSNLI
QMVTGMQEIK LNNCEKQKRW QWERIQVKLF KISVKGLALG QTQQAGSVFF NQTTNILISF
IAAKAVVEGD MTLGMMMSLT YIIGQLNGPI NAFIGFAQQL QDAKISLERL NEVHNREDEE
QDIGSKLQAL PERRDIVVDH VSFSYDGADR DYVLDDICLN IPEKKVTAIV GASGSGKTTL
LKLILGFYEP NRGNIRIGDT PVSLLNPHVW RAKCGSVMQD GFIFSDTIAN NIAVGEEHVD
RERLRRAVEV ANIRGFIDSL PLGYNTKIGM EGNGISQGQK QRLLIARAVY KNPEFLFFDE
ATNALDANNE REIMEHLQEF YRGKTVVIVA HRLSTVRDAD KIVVLDQGKI AEEGTHRELT
ERKGLYYRLV KNQLELGN
//
