ID A0A139WQN4_9CYAN Unreviewed; 533 AA.
AC A0A139WQN4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:KYC34737.1};
GN ORFNames=WA1_49300 {ECO:0000313|EMBL:KYC34737.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC34737.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC34737.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC34737.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
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:KYC34737.1}.
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DR EMBL; ANNX02000064; KYC34737.1; -; Genomic_DNA.
DR RefSeq; WP_017741192.1; NZ_KQ976355.1.
DR AlphaFoldDB; A0A139WQN4; -.
DR STRING; 128403.WA1_49300; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR PANTHER; PTHR30386:SF26; TRANSPORT PROTEIN COMB; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..156
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..258
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 59007 MW; 887958543234FC5E CRC64;
MSINNGNSNG NGNGNGNGNG NVRLPKLALA NIQQLEQNTN KESTIEPKPP STAPRYIPKF
DQPVILTQPR KWSRAILWSL MAVTAGAIIW ANVAKIEEAV SATGKLEPTG TVKEVQAPVG
GVVKQIHIED GQHVKSGERL LSLDPTTALA QLASLQKIRV SLVQENQFYQ SQLRGASSGV
IPLKIPNEMI DLTKSRAALI ADNQVYRAQL DGLRDPNRLT IEQKERLQSN RSELNARVAA
AKLEIVQLQH QRQQAEIKQA STIDTLAMNK GILNSVTPLM QDGAISKIQY FKQQQEVRNG
QSEIDQLVQE RARLNSAIFQ AQAKLQNTIA LSRQDWLQQI ADNNKRIAEI DSQLTKAIVE
NHKKIAEIDS QLSQTQMNLK YQEIKSPVAG TIFEIKAHTP GFVVTSSEPI LKVVPDDALI
AKVYITNKDI GFVFEGMTVD VRIDSFPFSE FGDIKGQLIS IGSDALPPDQ IYPYYRFPAK
VRLSQQSLLA NGRKIQLQSG MSVSTNIKIR ERTVMSIFTD MFSSSVESLK TVR
//
