ID A0A163XP47_9BRAD Unreviewed; 451 AA.
AC A0A163XP47;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=A4A58_15425 {ECO:0000313|EMBL:KZD21166.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD21166.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD21166.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD21166.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365093}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU365093}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|RuleBase:RU365093}.
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:KZD21166.1}.
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DR EMBL; LVYV01000053; KZD21166.1; -; Genomic_DNA.
DR RefSeq; WP_068737195.1; NZ_LVYV01000053.1.
DR AlphaFoldDB; A0A163XP47; -.
DR STRING; 943830.A4A58_15425; -.
DR OrthoDB; 9810980at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR010129; T1SS_HlyD.
DR NCBIfam; TIGR01843; type_I_hlyD; 1.
DR PANTHER; PTHR30386:SF17; ALKALINE PROTEASE SECRETION PROTEIN APRE; 1.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU365093};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU365093}; Membrane {ECO:0000256|RuleBase:RU365093};
KW Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW Transmembrane {ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 79..118
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
SQ SEQUENCE 451 AA; 49833 MW; 78E4182F6F4555C1 CRC64;
MKQYPLEEFT ADRSQSAAAP TAERSFRLWP RVLSGLALVV LLVFGCGGWA AIASLEGAVV
ASGIVRVDQN LKEVQHRDGG IVKMLAIRQG DLVGEGQVLA TLDDVQIRAE LLIVRSQLGE
ALGRQARLIA ERDNLPTIEF PADLGRVSSA ADIVMHGESR LFTGNKVGRD SQKEQLELSI
TQTLEEIKGM EARQVAKEEE IKLVGAERDK LDALFEKKIV EYTRVYSAHR DWARILGERG
EISAGIARAK VRASEIRVQI IAVDQNASTE AQRDLRTVDA RISELSERKL AIEDRLSRTE
IRSPVSGYVN ELFVHTVGGV ITPAAKIATI VPQNAELKFE IRISPADIDQ VREGQPARIR
LTAFNRTTTP EMKGRVTMVS PASARDSTNG QEHYIAYVNL LPTEDAIVQL NGMKLVPGMP
AEVFVSTQER TVASYLSKPF TDQMNRAFRE R
//
