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Database: UniProt
Entry: Q5FH47_EHRRG
LinkDB: Q5FH47_EHRRG
Original site: Q5FH47_EHRRG 
ID   Q5FH47_EHRRG            Unreviewed;       514 AA.
AC   Q5FH47;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN   Name=aprE {ECO:0000313|EMBL:CAI27603.1};
GN   OrderedLocusNames=ERGA_CDS_01510 {ECO:0000313|EMBL:CAI27603.1};
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI27603.1, ECO:0000313|Proteomes:UP000000533};
RN   [1] {ECO:0000313|EMBL:CAI27603.1, ECO:0000313|Proteomes:UP000000533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel {ECO:0000313|EMBL:CAI27603.1,
RC   ECO:0000313|Proteomes:UP000000533};
RX   PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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}.
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DR   EMBL; CR925677; CAI27603.1; -; Genomic_DNA.
DR   RefSeq; WP_011255335.1; NC_006831.1.
DR   AlphaFoldDB; Q5FH47; -.
DR   KEGG; erg:ERGA_CDS_01510; -.
DR   HOGENOM; CLU_023976_1_1_5; -.
DR   OrthoDB; 9810980at2; -.
DR   Proteomes; UP000000533; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.170; -; 1.
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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:CAI27603.1};
KW   Membrane {ECO:0000256|RuleBase:RU365093};
KW   Protease {ECO:0000313|EMBL:CAI27603.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU365093};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365093};
KW   Transport {ECO:0000256|RuleBase:RU365093}.
FT   TRANSMEM        76..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365093"
FT   COILED          326..353
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   514 AA;  57748 MW;  7BA1A71F8386F633 CRC64;
     MLKLLDNTYM YKKLKELVKT GFSLPKLLGH NTLHITNNEA PRKLHVLQKT LLIIDSIINF
     LFKYNKKDTS NEVLKISWGP LFTGFIVILL FFGVFGIWAA VAPLDGSVVA QGEVISSSEK
     QIVQHLEGGI IEKILVKEGE FVEKNQPIIY LHNTTAQANL DIIKERMLDM LATEARLTAI
     KYNYNHIKFP NSINNLSNKE IRDQIIKNQQ QLFESHQKNI SGQINILQQR TKQLHQELSG
     LSAQLTSATT QHQLINEELA AKKSLLADGY ISKPYIIALE RQYAESQGKI GQIESAIASV
     NQKIGENKLE IINITNNVQN KISIELKDTI SAIADLKERM KTAQDVLDRT VIRSPQSGII
     TGLKYHTEGG VIPPGAPITN VVPSDDNLIV DAKIQTRNIE EILSAQAKEV NMVSYENYKG
     LKAKVRLSAY NIRKVGLANG IVTQVSADAL TEANGMRYYK IQVIIPKEQS KKLKNLRLYP
     GMPAEVFIIT QSRTLLNYLF TPITSTFEKA FNER
//
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