ID Q31G29_HYDCU Unreviewed; 307 AA.
AC Q31G29;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=ATP-binding cassette superfamily transporter, permease component {ECO:0000313|EMBL:ABB41894.1};
GN OrderedLocusNames=Tcr_1299 {ECO:0000313|EMBL:ABB41894.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB41894.1};
RN [1] {ECO:0000313|EMBL:ABB41894.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB41894.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA Richardson P.;
RT "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000256|ARBA:ARBA00024202}.
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DR EMBL; CP000109; ABB41894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31G29; -.
DR STRING; 317025.Tcr_1299; -.
DR KEGG; tcx:Tcr_1299; -.
DR eggNOG; COG0601; Bacteria.
DR HOGENOM; CLU_036879_0_1_6; -.
DR OrthoDB; 9805855at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF6; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:ABB41894.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Nucleotide-binding {ECO:0000313|EMBL:ABB41894.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 134..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 227..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 273..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 95..292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 307 AA; 33900 MW; 0374C77F49F3C07C CRC64;
MIQYLVRLVL SVVLITWVVS SLVFLLIHLV PGDPVAVMLG DWASPTDEAL LRKQLGLDLP
LWQQYGHYMY GLLHGDLGQS LFYHQPVSEL IGERFPYTLK LAVMALLIAV LIAFPLGYWA
ALKADSWPDY FSMTVSLLGV SIPNFWLGPM LILVFSIGLA WLPVSGAEQP LSWLLPAITL
GTALSAILAR MLRASLLEIF HEDYIRTAQA KGLSSSRVYG QHALRNALLP VITILGLQLG
TLLGGAVITE VVFDWPGLGQ LLVDSIQRRD YPVVQACILV ISVAYITVNG LTEVVYAWLD
PRIRLAK
//