ID A0A2G2K0U7_9FLAO Unreviewed; 728 AA.
AC A0A2G2K0U7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:PHS04218.1};
GN ORFNames=COA88_14160 {ECO:0000313|EMBL:PHS04218.1};
OS Kordia sp.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=1965332 {ECO:0000313|EMBL:PHS04218.1, ECO:0000313|Proteomes:UP000221821};
RN [1] {ECO:0000313|Proteomes:UP000221821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PHS04218.1}.
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DR EMBL; NVVR01000066; PHS04218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2K0U7; -.
DR Proteomes; UP000221821; 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; 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:PHS04218.1};
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 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..128
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 174..453
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 487..722
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 728 AA; 82672 MW; 6C1BE8E6E02E2AF1 CRC64;
MKKFPSYIQT ESKDCGPTCI KIIAKYFKRS LSIQELRSLS ETTREGSSLL HLSDAAESIG
FRTLGVKVSF EHLKKAVFPC IIHWNNNHYV VVYKIKKNII YISDPGHGLI SYSKDDFLKF
WIGNNVTEKT EEGIALLIEP TAGFYDRDFK EDKKLNFSFL SNYVFKYKKL IVQLALGLLA
GSAMQLALPF LTKSIVDVGI KNQDVNFIYL ILAAQILLFL GKTSVDFIRS WIILHLSTRI
NISLVSDFFI KLTNLPISYF DVKMTGDLLQ RINDHKRIER ILTSSSLSVL FSLVNLMVFG
AVLFHYSSTI FSIFAVGSFC YFTWILFFFK RREELDYKNF SEASNEQSVV IELISGMQEI
KLHNAEKQKR WKWEHIQARL FKISIKSLAL EQTQSIGSNF INELKNILIT VFAAKLVIEG
SITLGMMMAI TYIVGQLNAP IVQLISFLRE LQDAKISLDR LSEIHMMDDE ETNKQEKIKT
LPEKRDIIIE NLSFRYTGSD KNVIDKLSLT VPQNKVTAIV GTSGSGKTTL LKLLLKYYEE
YTGEINLDTT ALKNIAQQTW RANCGVVMQD GFIFNDTIAN NIAIGETHID KEKLIYAVQT
ANIKEYIDQL PLGFNTKIGQ EGVGLSGGQK QRLLLARAVY KNPAFLFLDE ATSALDANNE
KVIMNNLDTF FKDRTVVVIA HRLSTVKNAD QIVVLEEGKI VEIGSHQELV ANRKNYFNLV
KNQLELAS
//
