ID A0A286H095_9PROT Unreviewed; 730 AA.
AC A0A286H095;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SOE00769.1};
GN ORFNames=SAMN05421508_11428 {ECO:0000313|EMBL:SOE00769.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOE00769.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOE00769.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOE00769.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCNJ01000014; SOE00769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286H095; -.
DR OrthoDB; 5288404at2; -.
DR Proteomes; UP000219621; Unassembled WGS sequence.
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:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18783; ABC_6TM_PrtD_LapB_HlyB_like; 1.
DR CDD; cd02259; Peptidase_C39_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:SOE00769.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000219621};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..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 403..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..141
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 173..452
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 486..721
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 730 AA; 79543 MW; 721E8AA931432D06 CRC64;
MEPAPTALEP VPAQAPSGLH VLAAVAAHHG VSLSADGLAR QYGLQQQEPS DKLLLRLLTE
AGFKAKAATL TWRELMRLGD EFPFIATVGR GRRVVLSGVR KRPGDGVEEI AIVDIVANPG
AFTFLTREEF ERVWGGQVIL VRRRTGALSE DRRFGLGWFL PLFHRERRTM TQVLVASVAL
VLLGLGIPIF FQIVIDKVLL HEARDTLAVL GLGIIGVVAF EAMMTYLRGT LLLHATTRID
ATVARRTFGH LVSLPLPFFE TSASGVLVKH MQQPEVIREF MSNKLINALI DMLALFVFVP
VLFWYDVRMA SLIVAFSLAS AAVIFVLLPI FRRALMRLYD AEGQRQSLLV EAIHGMRTVK
SLTLEPMLQR VWGARSAEAI QSHYDVAKVS ISARALVGLI EKLMVVAIIW VGASLVFAGD
LTVGGLVAIN MLAGRVSQPV SQLVALVNEF QQTSLSIRML GEIMNRRPET AGASTGGARP
KVKGGLRFED VTFAYPTSEA KALDGVSFDV PPGTTLGLVG RSGSGKSTIT RLIQGLYAPS
AGTIRIDGVD IREFDLGHLR RNVGVVLQDS FLFRGSVREN IAVGKPSASL LEVHEAAELA
GASEFIERLP QGYDTMLEEN AHNLSGGQRQ RLAIARALLV QPPILIFDEA TSALDPESEA
IVQANLSRIA EGRTLIVVSH RLSSLVHCDA ICVLDRGEVQ AVGPHRDLLR DSALYLSLWN
RQNQHLEAAE
//
