ID N9F5S0_ACIHA Unreviewed; 389 AA.
AC N9F5S0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Membrane fusion protein biotin-lipoyl like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F927_01611 {ECO:0000313|EMBL:ENW18173.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW18173.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW18173.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW18173.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) 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:ENW18173.1}.
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DR EMBL; APQQ01000020; ENW18173.1; -; Genomic_DNA.
DR AlphaFoldDB; N9F5S0; -.
DR PATRIC; fig|1217659.3.peg.1580; -.
DR HOGENOM; CLU_018816_15_1_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 2.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR PANTHER; PTHR30386:SF24; MULTIDRUG RESISTANCE EFFLUX PUMP; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
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 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..336
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT DOMAIN 337..380
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..254
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42178 MW; 9BFC8B060E97420E CRC64;
MAEETKDNTE KQTQESPAIN AETSPQSSNT IQAAEMPPPP PPASKLIKTK RSTLWWMLLV
LLVGITIILW AWKIGPFHTA IEQTDNSYIK GKTTILSSQI NGYIKDVLVK DFDHVKRGQV
LMHIDATTYD QKVTQAVSGV EQAQNSLANQ TQAIAQRQAD VVAAQAKLDQ VKAQYDLSLA
QLKRYQQLGN SGAASKSEQD KAAADAQNNL ALLKQAQANI LVAQEALKTA QVAEAGLKAQ
VNSAQAQLDQ ANTTKDYSTI VAPLDGQLGE VNPRVGQYVA AGSQLLYLIP QQTWVIANFK
ETQIANMKIG QKASFTVDAM KHQKFTGRVE QISPAAGSEF SVLKPDNATG NFTKVVQRIA
VRIAIDPDQE GIENLRPGMS VATSVDTDS
//
