ID A0A151BVH6_9MICO Unreviewed; 427 AA.
AC A0A151BVH6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Hemolysin {ECO:0008006|Google:ProtNLM};
GN ORFNames=AZH51_02895 {ECO:0000313|EMBL:KYH43856.1};
OS Branchiibius sp. NY16-3462-2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Branchiibius.
OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH43856.1, ECO:0000313|Proteomes:UP000075667};
RN [1] {ECO:0000313|EMBL:KYH43856.1, ECO:0000313|Proteomes:UP000075667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH43856.1};
RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT sample.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KYH43856.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVCF01000040; KYH43856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BVH6; -.
DR STRING; 1807500.AZH51_02895; -.
DR Proteomes; UP000075667; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000075667};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..180
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 199..260
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 266..323
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 427 AA; 45923 MW; 168F6820410779E9 CRC64;
MVVAFASVVA GFFLAAMESS LVRISKSQAR ELLEDGRRGA VQLVRLVDNR GPAAMVLAFL
RVGAEATAAV LVTLAADRIF EDFWVTLLVA IGVMALASFI LVGVSPRTFG QQHATAMALF
GAPVVSFFLT VLGPVARGLV AVGNAVTPGP GFRDGPFASE EELRDFVDMA TDSQLIEADE
RRMIHSVFEL GDTVAREVMV PRTDMVVIDK TKSLRSAMSL FLRSGFSRVP VVDDGPDDIE
GLVFLKDVAR RLTLNPDSAS LPVTEVAREV AFIPDSKPID DLLREMQTSR QHFAVVIDEY
GGTAGLITLE DIIEEVVGEI DDEYDRVAPG VEELPDGVIR IPARMPVDDL AELMDVTLED
DDVDTVGGLL AKLIGRVPIP GATAQIAGLQ LTADEMAGRR HQIATILVSR VVPDDEPSVE
HEEVAAP
//
