ID A0A0R1HJ20_9LACO Unreviewed; 438 AA.
AC A0A0R1HJ20;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Hemolysin {ECO:0008006|Google:ProtNLM};
GN ORFNames=FC66_GL001449 {ECO:0000313|EMBL:KRK45481.1};
OS Dellaglioa algida DSM 15638.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Dellaglioa.
OX NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK45481.1, ECO:0000313|Proteomes:UP000051450};
RN [1] {ECO:0000313|EMBL:KRK45481.1, ECO:0000313|Proteomes:UP000051450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK45481.1,
RC ECO:0000313|Proteomes:UP000051450};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRK45481.1}.
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DR EMBL; AZDI01000008; KRK45481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1HJ20; -.
DR STRING; 1423719.FC66_GL001449; -.
DR PATRIC; fig|1423719.4.peg.1473; -.
DR Proteomes; UP000051450; 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; 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:UP000051450};
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 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..195
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 214..274
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 279..336
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 438 AA; 49780 MW; 1D9810EBC47F9675 CRC64;
MTLFAAAFFV AAEFALVQAR PSAIEADMEA GIGNRKKQER ALKMLAHLNE YLSTTQVGVS
VAGIILGWVG EKTIEFLLVD VLKWFHFASE SGLNIIGAII GVLILTYVEV VYTEIVPKNL
SIDMPVQVLM VVLTPLRYFH LAFYPLVWLL NNSATRVARM LGITPTDENS EIFTQKEILA
LSQNAVSGGE LDRDDYVYMQ RAFDLNDKIA KDIMVDRTSL YVVDITDTIH DVIKDYLHQG
YSRFPVVANN DKDKILGYVY IYDLVRQAEI DDTILISKML RSIITVPETT PIRTLLSQMI
SKQTPIVVVS DEYGGTSGIV TDKDIYEELF GTVKDEIDDV SSEYIVKNDD GTYNVSGKTT
LYDFERFFKI KNKEMNDSES VTLAGFILEN HKVRLNEVIR FDAFDFKIIE FKRNYIDWFQ
VSYSSKQPET TEEEKISK
//
