ID A0A2R5F9D1_9PROT Unreviewed; 462 AA.
AC A0A2R5F9D1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN Name=hasE {ECO:0000313|EMBL:GBG14429.1};
GN ORFNames=NMK_2028 {ECO:0000313|EMBL:GBG14429.1};
OS Novimethylophilus kurashikiensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Novimethylophilus.
OX NCBI_TaxID=1825523 {ECO:0000313|EMBL:GBG14429.1, ECO:0000313|Proteomes:UP000245081};
RN [1] {ECO:0000313|EMBL:GBG14429.1, ECO:0000313|Proteomes:UP000245081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=La2-4 {ECO:0000313|EMBL:GBG14429.1,
RC ECO:0000313|Proteomes:UP000245081};
RX PubMed=29411502; DOI=10.1111/1462-2920.14062;
RA Lv H., Sahin N., Tani A.;
RT "Isolation and genomic characterization of Novimethylophilus kurashikiensis
RT gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of
RT Methylophilaceae.";
RL Environ. Microbiol. 20:1204-1223(2018).
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:GBG14429.1}.
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DR EMBL; BDOQ01000007; GBG14429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5F9D1; -.
DR Proteomes; UP000245081; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
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.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
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:GBG14429.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:GBG14429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245081};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT DOMAIN 82..123
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 235..298
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 462 AA; 49634 MW; 3DB64E9E6BC8768C CRC64;
MKSPIESLVS WINSFNPYSP DKLAPAAGGN PLPLTTEGSN SKMPWVFAGF FVAFAGWAVI
APIDSGVVLN GVVVVQGNRK VVQHPLGGVV SSIMVKEGSH VRAGDLLFKL NPLNTEANLA
GAEVDYIEAL VTESRLKSER EGAPEIRWDA DLAPYTKDPR FEAAKAVQTG LFMARKGELK
AQQGALSQQI AGLKAQNAGL EESQAPRTQQ IALLSEEVRN NRELAAEGHV PRARVSELER
QLAEANVSLS EMQAEKGKNL TAIAGLEFQL AQSKATWLKE LETQLVDAEK SHISLKAKVA
SFKSELAQTD VRAPAAGIVV GLKVNTVGGV VAPGQTQMEI VPEDSPLIVE ADVPTNMIDK
VHAGLLADLR FSAFNTISTP VVAGRVKLVG ADRQLAQPPV HPNDYYLAQV ETSAQGVRQL
DGKVIQAGMP VEVVVKTGER SFMSYLLKPL QDRLARSFKE GM
//
