ID C5RYU5_9PAST Unreviewed; 426 AA.
AC C5RYU5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Membrane fusion protein (MFP) family protein {ECO:0000256|RuleBase:RU365093};
GN ORFNames=AM305_04368 {ECO:0000313|EMBL:EER48169.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER48169.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER48169.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER48169.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004377, ECO:0000256|RuleBase:RU365093}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004377,
CC ECO:0000256|RuleBase:RU365093}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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:EER48169.1}.
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DR EMBL; ACQL01000020; EER48169.1; -; Genomic_DNA.
DR RefSeq; WP_005822077.1; NZ_ACQL01000020.1.
DR AlphaFoldDB; C5RYU5; -.
DR eggNOG; COG0845; Bacteria.
DR OrthoDB; 9775513at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 2.40.30.170; -; 1.
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:SF25; MANNURONAN SYNTHASE; 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; 1.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365093};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365093};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365093};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365093}.
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365093"
FT DOMAIN 90..134
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47694 MW; FDBD8EE36AB25B1E CRC64;
MNKDKTPHDT VEKLQTKQAA KKQAPLNKKD LRLLNDLNAA LQQENHHSIF ATISFFFALM
VIFVIWAYNS PIDEVTRGQG SIIPNSREQV IQSLDPGILK EMLVKEGDTV EKGQVLLKLD
DTRSSAILRE SQAKVENLEA LSARLQAEAY GTPLVFSEKI PASLQERERI IYEKRKTSLQ
ESLASLQNSK NLLDREIRIT EPIVAKGAVS AVELLRMKRQ STDLQLQMVE RKNKYVTDAS
AELTKIEAEL SQARENMAMR ADPVERSLIR SPLKGIVKNI RINTIGGVIS AGQDIMEIVP
IEDTLLVEAY ISPSDVAYVR PGMTALVKLT AYDYAIYGGL EGTVTLLSPD TLHDQKRPSD
LKLNPNEAYY RVLVKTEGSH LTDKDGKVMP IIPGMIASVD IKTGQKTVFQ YLIKPITRMK
QSLQER
//
