ID A0A110BK55_9FLAO Unreviewed; 741 AA.
AC A0A110BK55;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:CVK16019.1};
GN ORFNames=Ga0061079_104138 {ECO:0000313|EMBL:CVK16019.1};
OS Apibacter mensalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK16019.1, ECO:0000313|Proteomes:UP000182761};
RN [1] {ECO:0000313|EMBL:CVK16019.1, ECO:0000313|Proteomes:UP000182761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53146 {ECO:0000313|EMBL:CVK16019.1,
RC ECO:0000313|Proteomes:UP000182761};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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; FCOR01000004; CVK16019.1; -; Genomic_DNA.
DR RefSeq; WP_055425228.1; NZ_LIVM01000004.1.
DR AlphaFoldDB; A0A110BK55; -.
DR STRING; 1586267.GCA_001418685_00857; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000182761; 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 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:CVK16019.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000182761};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 184..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..140
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 185..466
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 499..735
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 741 AA; 84740 MW; 7809B8DD3210D457 CRC64;
MKLLKIFNKS KVIFYHQLES TDCGAACLAM IMSYYGNRSS LSSVKALFEF TRLGISVQDI
LDVSEKVGLY SVALKLTLTE LEEIPLPCIL YWKQSHFVVI KKIGKKNKQT FYHILDPGYG
KIILEQEVFE TEWKGNSEKG VAIYLEPTEN FAIGKKKDKE EKGLINSNIF KFSISFIKKN
KSKYIISFIL IVLGLVTNWF IPFTFQKIID IGILSKSISV VYYLLLAQFI LFISNFLSDF
INQLILTKSN FLLTINLKRA LLNKLLKLPL NFFDTKINTE ILQRLNDQNT IQNFITWKGI
NLILILFNIL VFGGILFYFN RFIFFVYLVL SILSILWVLI FLKRRRINEY AIFLKQTENS
NNIYEFIMNM PEIKINGAQN NIINKILYIQ DKSNKLELRS LFLNTYQLVG MNIFSKLKEI
IAIGYCAILI IEGKMTLGVL LSISYIIGQL TGPIQNIISF IRDVQDVNIA NKRIELLYDT
PNEDDTNKIE IKNYNIKNIN VNSVSFKYPG SYNPFILENV SFNIPKNSVT AIVGASGSGK
TTLLKLLLSY YPVKQGGIYL DDYSINEINA EDWRDKCGTV LQNGNIFSDT IASNISMSME
DCNIDQLRES AKIAGIQDFI EQLPMHYFTR IGNSGIELSG GQKQRILIAR AVYKNPNYLF
FDEATSALDS ENEKIIHDNL QEFFKGRTVV IIAHRLSTVK NADQIIVLKN GQIAEVGNHN
QLVKAKSEYY NLVKNQLELG A
//
