ID A0A2A3HAG5_9ACTN Unreviewed; 443 AA.
AC A0A2A3HAG5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Hemolysin {ECO:0008006|Google:ProtNLM};
GN ORFNames=BKI49_04975 {ECO:0000313|EMBL:PBC65009.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC65009.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC65009.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC65009.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:PBC65009.1}.
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; MLCE01000006; PBC65009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3HAG5; -.
DR Proteomes; UP000217789; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; PTHR43099:SF6; UPF0053 PROTEIN RV1842C; 1.
DR PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000217789};
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 DOMAIN 1..203
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 222..282
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 287..343
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 443 AA; 47226 MW; D424ECE67663368F CRC64;
MTIPLLLLGA AFLLILANGF FVAAEFGLVT VERPDAEKAA AEGDRRAGTV VDSLKELSFQ
LSGTQLGITI TSLVVGMLAE PALAELLHGP FTAIGLPEGA VPGVAVVVGM LLASAVQMVV
GELVPKNWAV SRPLQVARFV AGPQHAFSRL FRPVIAALNT VANRLVRALG VEPAEELASA
RTPGELVSLA RHSAQAGALE QDTADLFVRT ISLADLTAQH VMTPRVKVSA LQSSATAEDV
VNLTRATGLS RFPVYRERID EIVGMVHLKD ALAIPSHDRR RTPVGRIAQA PLLVPETLPV
QPLLEQLRSE QPIAVVVDEY GGTAGVVTLE DIVEELVGEV HDEHDDVLNE LPELAPAPPE
DGRPAWDADG SCRVDVLQRI GIDVPEGPYE TVAGLVADLL GRIPAPGDRA ELPGWRLSVR
QVGHYRAERV RLVRTAPVPE AVR
//
