ID A0A127R3C7_9BURK Unreviewed; 709 AA.
AC A0A127R3C7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ABC transporter family protein {ECO:0000313|EMBL:AMP16465.1};
GN ORFNames=CPter291_4235 {ECO:0000313|EMBL:AMP16465.1};
OS Collimonas pratensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP16465.1, ECO:0000313|Proteomes:UP000074914};
RN [1] {ECO:0000313|EMBL:AMP16465.1, ECO:0000313|Proteomes:UP000074914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter291 {ECO:0000313|EMBL:AMP16465.1,
RC ECO:0000313|Proteomes:UP000074914};
RA Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT "Exploring the genomic traits of fungus-feeding bacterial genus
RT Collimonas.";
RL Submitted (NOV-2015) 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; CP013236; AMP16465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127R3C7; -.
DR PATRIC; fig|279113.10.peg.4221; -.
DR Proteomes; UP000074914; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18567; ABC_6TM_CvaB_RaxB_like; 1.
DR CDD; cd03246; ABCC_Protease_Secretion; 1.
DR CDD; cd02419; Peptidase_C39C; 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; IPR033838; CvaB_peptidase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF606; COLICIN V SECRETION-PROCESSING ATP-BINDING PROTEIN; 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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..137
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 171..450
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 485..709
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 709 AA; 78480 MW; 3D18D42EF8723616 CRC64;
MFNRLAFGIH ATLPLMLQTE ATECGLACLG MVAGYHGYRT DLASLRRRFP VSLKGSTLRD
LIAIAEQLEL ASRPLKLDLD DLAQLKLPCV LHWNLNHFVV LQEVGLRFAT VYDPAFGIRK
LSLAEVAKAF TGVALELWPN PGFKPARAVE SVPLRRLLGR ISGLYRSFSQ ILLLSLALEV
FAVVSPFFLQ WVIDNVLVAA DRDLLTTLAL GFGLLMLMQQ AIGVGRSWVL MYMSTTLNVQ
WQANVFTHLL RLPVAYFEKR HLGDVVSRFG AVGIIQHTLT TSFLEAILDG VMTVATLALM
FIYSPTLAWI AIAAMLLYGL GRWAWFAPLR HATEEQIIHA AKQQTHFLET IRGVKTIKLF
QRQDERRSTW LSLLVDQINA DLRTQKLSLL YKTLNGVLFG IENILTIWLG ARLVMDGNFT
VGALMAFTAY KGQFDSRVSS LIDKFVELKM LQLQGERLAD IVLQPPETTH GCNLGEQEAM
LSPSLEVRGL RFRYAEQEPY VLDDVSFRIE AGESVAIVGP SGGGKTTLVN VLLGILAPSQ
GEVLIGGQPV QQVGLDTLRR MVGTVLQDDV LFAGSLADNI SFFDPQADQA WIRQCARLAA
IEQDIGAMPM GYNTLVGDMG TILSGGQKQR ILLARALYKR PQILFLDEAT SHLDIEREQQ
VNHAIGAMRI TRVIVAHRPE TINSADRVIM LVDGKVIELA VQAQQAASA
//
