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Database: UniProt
Entry: A0A0T7BQ66_9CYAN
LinkDB: A0A0T7BQ66_9CYAN
Original site: A0A0T7BQ66_9CYAN 
ID   A0A0T7BQ66_9CYAN        Unreviewed;       424 AA.
AC   A0A0T7BQ66;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Lipoprotein {ECO:0000313|EMBL:AKG21224.1};
GN   ORFNames=IJ00_07875 {ECO:0000313|EMBL:AKG21224.1};
OS   Calothrix sp. 336/3.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG21224.1, ECO:0000313|Proteomes:UP000065745};
RN   [1] {ECO:0000313|EMBL:AKG21224.1, ECO:0000313|Proteomes:UP000065745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:AKG21224.1,
RC   ECO:0000313|Proteomes:UP000065745};
RX   PubMed=25614574;
RA   Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA   Battchikova N.;
RT   "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT   cyanobacterium isolated from a finnish lake.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the UPF0194 family.
CC       {ECO:0000256|ARBA:ARBA00010602}.
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DR   EMBL; CP011382; AKG21224.1; -; Genomic_DNA.
DR   RefSeq; WP_035151736.1; NZ_CP011382.1.
DR   AlphaFoldDB; A0A0T7BQ66; -.
DR   STRING; 1337936.IJ00_07875; -.
DR   KEGG; calh:IJ00_07875; -.
DR   eggNOG; COG0845; Bacteria.
DR   OrthoDB; 9778236at2; -.
DR   Proteomes; UP000065745; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   PANTHER; PTHR32347; EFFLUX SYSTEM COMPONENT YKNX-RELATED; 1.
DR   PANTHER; PTHR32347:SF23; UPF0194 MEMBRANE PROTEIN YBHG; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   PRINTS; PR01490; RTXTOXIND.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipoprotein {ECO:0000313|EMBL:AKG21224.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..118
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   DOMAIN          224..379
FT                   /note="RND efflux pump membrane fusion protein barrel-
FT                   sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16576"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          261..288
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   424 AA;  46202 MW;  16555F092F9C9970 CRC64;
     MSQTINSAKP ITTPPKSDEP KIPTPKKPRR WLWILGGTVA IASVGFGVWY GFFRPQPANI
     IQFNGRIEGY ETDVSTKGIG RVEEVTVREG DTVKKGQLLV RLSDEEVQSE LSAATAQVNA
     AKQREAYARL QISILADQLA DANLNLQQSQ GDTQGKVAEA NALVSTAKAV VKQEQARVLE
     ARALVEQARV DSDRYAHLAI EGAETKQRYE VARTVYNTAK AALQSRLAAV EAAQTAVNIA
     QGKLTQAQTT TLNPGRQQTN VSRFETQAQQ ARNTIAAAQA DVKTAQANQQ LIQSRLNNLT
     VKSPIDGVVT TRSVEPGTVV LPSRPLLRVV DLSQVYLRGF IPGGQIAQVR VGQLANVYLD
     NDPKHQKSFK ATVTAIDSKA SFTPENVYFQ SDRVQQVFGV KLSLEQRERL AKPGMPADGE
     IPLN
//
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