ID A0A0F7K297_9GAMM Unreviewed; 397 AA.
AC A0A0F7K297;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:AKH21659.1};
GN ORFNames=AAY24_16335 {ECO:0000313|EMBL:AKH21659.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21659.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH21659.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21659.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(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}.
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DR EMBL; CP011412; AKH21659.1; -; Genomic_DNA.
DR RefSeq; WP_046860580.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7K297; -.
DR KEGG; seds:AAY24_16335; -.
DR PATRIC; fig|1543721.4.peg.3373; -.
DR OrthoDB; 9800613at2; -.
DR Proteomes; UP000034410; Chromosome.
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:UP000034410};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002517793"
FT DOMAIN 68..298
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT DOMAIN 299..366
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT REGION 376..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..167
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 380..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 42270 MW; 7E0A385C01053ABA CRC64;
MPVLSRYRGG ILILLLALLA SGCNGSDSTS SESAVAPAAP VPVVGVQEVR QQSLVLNTEL
AGRTTAYRIA EVRPQVTGII VERTFQEGGE VKAGQTLYRI DPARYQAAYD SAKSTLARDQ
AALTTARLKV KRYANLLKTK AVSQEAYDEA RAALQQAQAT VAMDEAALQA ARIDLDYTQV
SAPIDGRIGR SAVTQGALVT GNQTTALATI RQLDPIYVDV TQSSAELLRL KKALGEGELQ
RPEGFSAPVE LILEDGSRYP HPGKLEFSEV SVDESTGSVT LRALFPNPDQ QLLPGMYVRA
QVQNGVREGA ILVPQQAVSR DAAGRTTALV LNGDDQVEKR SLTVSRAVGN QWLVEEGLTV
GERLIVDGLQ KIQPGDTARA TPLTAETTPG SGVSTPN
//