ID A0A239A1M5_9FLAO Unreviewed; 730 AA.
AC A0A239A1M5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SNR89460.1};
GN ORFNames=SAMN06265376_10485 {ECO:0000313|EMBL:SNR89460.1};
OS Dokdonia pacifica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNR89460.1, ECO:0000313|Proteomes:UP000198379};
RN [1] {ECO:0000313|EMBL:SNR89460.1, ECO:0000313|Proteomes:UP000198379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25597 {ECO:0000313|EMBL:SNR89460.1,
RC ECO:0000313|Proteomes:UP000198379};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZNY01000004; SNR89460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239A1M5; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000198379; 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SNR89460.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..129
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 176..455
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 489..724
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 730 AA; 83006 MW; 718FF60E3AE0F45A CRC64;
MKKFPFYKQA DSKDCGPTCL KMIAKYYKKP IPIQLLRSLS ETTRSGSSLL GISNAAEKLG
FRTLGVKITL EQLKEEVPLP CILHWNKNHY VVLYKISRGV YHISDPAHGI LKYTKEELLK
FWIGNNATDA TAEGIALLLE TTPKFYEENF DEEKKNFGFS FIFKYVFRYR KFIVQLVIGL
LAGSLLQVVF PFLTQSVVDV GIKTRDINFI YLILIAQVAL FLGRTGVEVI RSWILLHLST
RINISLISDF FIKLMNLPIS FFDVRMTGDI LQRINDHRRI ERILTTSSLN VLFSMVNLVV
FGFVLAYYSF QIFGIFLLGS VLYFFWIVIF LKKRADLDYK RFSQVSQEQS KVIELINGMQ
EIKLHNAEKQ KRWSWEFMQA RLFKISIESL ALEQYQSVGS GFINELKNIL ITILSATLVI
NGDLLLGEMF AVTYIVGQLN SPISQLISFI RELQDARISL DRLGEIHNKE DEEGREETKI
TDIPDNADFD VKDISFRYIG SDVKVIDGLS LHIPANKVTA IVGVSGSGKT TLMKVLLKFY
EPNEGQIKIG SADLQNISQY SWRASCGVVM QEGYVFNDTI ANNIAVGDDH VNKKKLAHAV
DVANIKEFIE SLPLSYNTKI GMEGVGLSTG QKQRLFIARA VYKDPNFLFF DEATSALDAN
NEKVIMEKLD EFFKNRTAVV IAHRLSTVKN ADQIVVLDQG KIVEVGNHKT LTREKGYYYN
LVKNQLELGS
//
