ID A0A1N6X7W3_9FLAO Unreviewed; 719 AA.
AC A0A1N6X7W3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SIQ98369.1};
GN ORFNames=SAMN05880574_1446 {ECO:0000313|EMBL:SIQ98369.1};
OS Chryseobacterium sp. RU37D.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1907397 {ECO:0000313|EMBL:SIQ98369.1, ECO:0000313|Proteomes:UP000185978};
RN [1] {ECO:0000313|Proteomes:UP000185978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU37D {ECO:0000313|Proteomes:UP000185978};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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; FTMM01000044; SIQ98369.1; -; Genomic_DNA.
DR RefSeq; WP_076447874.1; NZ_FTMM01000044.1.
DR AlphaFoldDB; A0A1N6X7W3; -.
DR STRING; 1907397.SAMN05880574_1446; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000185978; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043214; F:ABC-type bacteriocin 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; cd18570; ABC_6TM_PCAT1_LagD_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; IPR005897; Pept_C39_ABC_bacteriocin.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR01193; bacteriocin_ABC; 1.
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:SIQ98369.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000185978};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..133
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 164..445
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 478..713
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 719 AA; 80915 MW; 79A730EC5536F34B CRC64;
MKKNILIRQH DIKDCGAACL ASVAIHYGLK MPIAKIRQIC HTDTRGTNVL GLIQGLEQMG
FNAKGVKGGI DALPELPLPA ITHVIVNGQM HHYVVVYKVA KDKITVMDPA RGKLEDYKIE
EFSKIWTGVL ILLEPNEYFE QRDEKTSLYK RFWNLVQPHK SILIQALLGA LVYTILGLST
SIYIEKITDY VLIDGNKRLL NLLSVGMIVI LLFQIFIGAM KSVLVLQTGQ KMDKHLILGY
YKHLLKLPQR FFDTMKVGEI ISRVNDAVKI RTFINDVSIQ IFVNIFIIIF SFALMFTYYW
KLALITALVI PFYFLVYWIT NKLNKKAERQ LMEESAELES HLVESITSVK TIKQFGVETF
ANNKTDNAFS KLLKTIYASV MNALFSGNSS EFLSRIFTII LLWVGSGYVI DRVITPGELL
SFYALIGYFT SPVSQLIGMN KTIQNALIAA DRLFEIMDLE REENTDKLDL KAENMGDILF
KEVSFSYGSR ADIFTGFNCQ IKKGETTAIV GESGSGKTTL ASLVQNLYSL KAGKIMIGDY
DINYISNYSL RNLVSVVPQQ IDLFSGNVIE NIALGEDFPD IQRILNITKN LGILSFVEKL
PNGFQTYLGE NGALLSGGQK QRIAIARALY KNPEILILDE ATSSLDTESE MVIQNTLQEF
RNQGKTMIVI AHRLSTIANA DTILVMKEGQ IIEKGNHNEL LNKNSVYKSM WEKQGTKLG
//
