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Database: UniProt
Entry: Q98BK0_RHILO
LinkDB: Q98BK0_RHILO
Original site: Q98BK0_RHILO 
ID   Q98BK0_RHILO            Unreviewed;       358 AA.
AC   Q98BK0;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Hemolysin {ECO:0000313|EMBL:BAB51972.1};
GN   OrderedLocusNames=mlr5537 {ECO:0000313|EMBL:BAB51972.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51972.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB51972.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- SIMILARITY: Belongs to the UPF0053 family. Hemolysin C subfamily.
CC       {ECO:0000256|ARBA:ARBA00006446}.
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DR   EMBL; BA000012; BAB51972.1; -; Genomic_DNA.
DR   RefSeq; WP_010913310.1; NC_002678.2.
DR   AlphaFoldDB; Q98BK0; -.
DR   GeneID; 66680345; -.
DR   KEGG; mlo:mlr5537; -.
DR   PATRIC; fig|266835.9.peg.4402; -.
DR   eggNOG; COG1253; Bacteria.
DR   HOGENOM; CLU_015237_3_1_5; -.
DR   Proteomes; UP000000552; Chromosome.
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; 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:SF27; MAGNESIUM AND COBALT EFFLUX PROTEIN CORC; 1.
DR   Pfam; PF00571; CBS; 2.
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.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          104..163
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          194..251
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  38852 MW;  8DBCF3FDA4DBE02F CRC64;
     MNDTPETAAR PDAGSAPKAS DTSEEGSSPS TVTGSAASEL SPAGPSLFDR VLGLFRQRNG
     TSLREEIAGA LAETASDAES FSPGERAMLN NILRLREVRV EDVMVPRADI EAVEITTTLG
     DLLGTFEQSG HSRMPVYSET LDDPRGMVHI RDVLAHITKL ARVKKGRTTR KTPVATQLDL
     AQVDLARTIG ELNLIRQVLF VPPSMLASDL MGRMQTTRTQ MALVIDEYGG TDGLVSLEDI
     VEMVVGDIED EHDDDEPMIT QAGDGVFIVD GKAEIDEVAK MIGEDFAAGE HGEYVDTIGG
     MIFNTLGRVP ARGEVVQAIP GFEFHVLDAD PRRVKRVRIV QSQKGERRRR ATARTEQA
//
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