ID A0A119CUV6_THIDE Unreviewed; 403 AA.
AC A0A119CUV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:KVW94249.1};
GN ORFNames=ABW22_12730 {ECO:0000313|EMBL:KVW94249.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW94249.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW94249.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW94249.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004519}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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:KVW94249.1}.
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DR EMBL; LDUG01000036; KVW94249.1; -; Genomic_DNA.
DR RefSeq; WP_059757263.1; NZ_LDUG01000036.1.
DR AlphaFoldDB; A0A119CUV6; -.
DR STRING; 1123392.GCA_000376425_02964; -.
DR PATRIC; fig|36861.3.peg.2331; -.
DR OrthoDB; 9783047at2; -.
DR Proteomes; UP000064243; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR PANTHER; PTHR30158:SF3; MULTIDRUG EFFLUX PUMP SUBUNIT ACRA-RELATED; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007161795"
FT DOMAIN 42..366
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 69..298
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..174
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 403 AA; 42039 MW; 10C5CE89882D8BCA CRC64;
MQIHRKLMFK PLGFALASVF LLAACGGNEQ QNAAGAAGQT APVVTVLTVQ VESVPVASEL
PGRTTPYLIA ELRPQVTGIV KQRLFKEGSE VKAGQVLYQI DPATYQAATD SARASLARAE
ANLDAARLKA ERYAELVKIE AVSKQANEES VAAMKQAQAD VGSAKAALDR ARIDLGYTRV
ASPIAGRIGR STVTPGALVT ANQVAALATV QQLDPIYVDL TQSSTELLHM KRDLESGKLQ
RAGGGAVPVQ LVLEDGSVYG VAGKLAFSEV TVDQDTGSVT LRAVFPNPKG ELLPGMYVRA
RLAQGVQDNA ILVPHAAVSR DPKGNATVML VNAESKVEPR IVKAPQSLGD QWVVTEGLAA
GDRVIVEGLQ KVKPGVQVEA QDAAAAQAPP AAPGVAPAAK RGS
//
