ID A0A1Q3S4Q3_9FLAO Unreviewed; 736 AA.
AC A0A1Q3S4Q3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ABC transporter ATP-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BGO42_07655 {ECO:0000313|EMBL:OJV71378.1};
OS Flavobacterium sp. 40-81.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1896169 {ECO:0000313|EMBL:OJV71378.1, ECO:0000313|Proteomes:UP000185767};
RN [1] {ECO:0000313|EMBL:OJV71378.1, ECO:0000313|Proteomes:UP000185767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=40-81 {ECO:0000313|EMBL:OJV71378.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV71378.1}.
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DR EMBL; MKTM01000020; OJV71378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3S4Q3; -.
DR STRING; 1896169.BGO42_07655; -.
DR Proteomes; UP000185767; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..135
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 180..461
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 494..730
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 736 AA; 83567 MW; F55C21B9B92E2451 CRC64;
MFRKPKVEFS HQLESTDCGA ACLCMIMSYY DKKVTLSQIK GLFEFTRVGV SIQDIIRTSE
KIGLISVPLK LTQAELEQIP LPSILYWRQE HFIVLEKIEI RKGERYYHLA DPAYGRIILD
SESFIKEWCG NNEKGVGIVL EPSDDFLAFS FPKETKKSIT ASPFFKTALA FLAKNKAKYI
GSILFILISL ATNFCIPFIF QRIIDTGITP KVIAVVYYLL LAQLVLFVSG FIADFISHLI
LTKINFQLSI SLKKDLLSKL MRLPIHFFDT RLNTETLQRL NDQNKIQNFI TWKGIELALN
VMNILVFGAI LCYFNFWIFS MYFSLSILSV IWVLFFLKKR AVLEYALFLG QSENSNNIYE
FIMNMPEIKI NDAQNKIITK ILTIQQKINR LELRSLFLNT YQLVGVNFLS KLKEIIAIAI
CAIFIINNQM TLGTLLSITY VIGQLINPVQ SLVSFVRDAQ DANIANKRIG EIYNNSDEDN
QNKEHIEHRI FQEISLENVS FKYPGNFNRF VLDNISLQIP NNSVTAIVGA SGSGKTTLLK
LLLSYYPVSD GMITLDELNI NNVYSNEWRK KCGIVLQDGT IFSGTIAENI ALAEETIVEE
KLINAAGIAC ILEFIEELPM GFNTKIGNAG IELSGGQKQR ILIARAVYKN PHYIFFDEAT
SALDADNEKK IHDNLQEFFK GKTVVIIAHR LSTVKNADNI IVLKEGQIVE QGIHQDLVSN
RAGYFNLVKN QLELGE
//