ID F2F6J2_SOLSS Unreviewed; 442 AA.
AC F2F6J2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Hemolysins {ECO:0000313|EMBL:BAK15434.1};
GN OrderedLocusNames=SSIL_1011 {ECO:0000313|EMBL:BAK15434.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK15434.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK15434.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK15434.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
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 -!- SIMILARITY: Belongs to the UPF0053 family.
CC {ECO:0000256|ARBA:ARBA00006337}.
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DR EMBL; AP012157; BAK15434.1; -; Genomic_DNA.
DR RefSeq; WP_008406006.1; NC_018065.1.
DR AlphaFoldDB; F2F6J2; -.
DR STRING; 1002809.SSIL_1011; -.
DR KEGG; siv:SSIL_1011; -.
DR PATRIC; fig|1002809.3.peg.1024; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_0_9; -.
DR Proteomes; UP000006691; Chromosome.
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; UPF0053 PROTEIN YRKA; 1.
DR PANTHER; PTHR43099:SF2; UPF0053 PROTEIN YRKA; 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 3: Inferred from homology;
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:UP000006691};
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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..344
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 442 AA; 49966 MW; BD2638EF4D65C516 CRC64;
MDVNTILNII LLIIFLGLTG FFVAAEFAVV KIRKSRIDQL ILEGNKKAVI AKKVAGDLDY
YLSACQLGIT ITAIGLGAFT KPYVKELLYP VFDWLNVSDV VASAASYVIA LAIVSYLHVV
IGEMAPKTLA IQFSEKVTLM LAGPLYWFGK IMYPFIQALN GTSRLLLRAV GVKSASEEQA
YSEEELKIIM AQSFQGGQID QQELKYLENV FAFDERVAKD IMVPRTDLVT IDKDMSAEEI
IQILDEHNYT RYPIVENNDK DRIIGVINAN KLLSYIVSNR TVQLEQFLTK VPFVLGVTSI
QDALLKMQKA KVHMTVIIDE YGGTAGVLTM EDVLEELVGE IRDEFDEDEV DDIRKSGENE
YTINGRVLLD ELEDRFGFEF EDSEEIDTIG GWIQHTNIDS IKNGEELQIG DEIKFDDHIW
VISDMDNYQI KEVVLRQYKL QQ
//
