ID A0A031LXP2_9GAMM Unreviewed; 389 AA.
AC A0A031LXP2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:EZQ12530.1};
GN ORFNames=CL42_00760 {ECO:0000313|EMBL:EZQ12530.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ12530.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ12530.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ12530.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:EZQ12530.1}.
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DR EMBL; JFYL01000001; EZQ12530.1; -; Genomic_DNA.
DR RefSeq; WP_035263863.1; NZ_JFYL01000001.1.
DR AlphaFoldDB; A0A031LXP2; -.
DR eggNOG; COG0845; Bacteria.
DR Proteomes; UP000023816; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30469:SF15; HLYD FAMILY OF SECRETION PROTEINS; 1.
DR PANTHER; PTHR30469; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..104
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT DOMAIN 123..303
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT COILED 91..201
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 389 AA; 43388 MW; 3F19B67CC65DDDFD CRC64;
MRILKQRKWW ILILLISMGG IYFIFRWWQG PVVETYLIEE KPLIQTVVAS GRAENVARSE
IGSEISGVVI ERRVQEGQRI AAGDVLLIIQ SDDLKAQVRE AEVALEELRK IRYPQAQVEL
KTAEFQLQQA SREARRRQQT EPGVLSVEEK EQALEAERLA RNQLSAAKLK AQSLAPGQVE
EKTLSERLNA LRAQLAKSEI RAQVSGTILT REVEKGDAIQ PGKVLFTVAV DSPTQIKVAV
DEQNLPYLKL GQKAEVIADA YPEQAFPAEV NFIAPNIDPQ RGTVEVKLAV NSVPNFLKQD
MTVSVNVETA RRNKTKVIAN DALIDPSTTQ AEVMVVREGK VQRQSVKLGL RGTAMSEILS
GLDHNDQVVI KPDQVKADQR VRTKQVQAL
//
