ID J9Z8A3_LEPFM Unreviewed; 477 AA.
AC J9Z8A3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative hemolysin {ECO:0000313|EMBL:AFS52725.1};
GN OrderedLocusNames=LFML04_0487 {ECO:0000313|EMBL:AFS52725.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52725.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS52725.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS52725.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002919; AFS52725.1; -; Genomic_DNA.
DR AlphaFoldDB; J9Z8A3; -.
DR STRING; 1048260.LFML04_0487; -.
DR KEGG; lfi:LFML04_0487; -.
DR PATRIC; fig|1048260.3.peg.523; -.
DR HOGENOM; CLU_015237_4_0_0; -.
DR Proteomes; UP000006177; Chromosome.
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:SF33; UPF0053 PROTEIN YEGH; 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}; 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 26..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..226
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 245..304
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 309..366
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 54211 MW; 4CAD4D6CEC2C9B30 CRC64;
MKTFRCIERK IIPNFERTFS FTMVPVWIDL FAIVVLIVIN AFLAASELSI ISIRMSRVHQ
MAQSGSPETL AIERLRKDPE KFVATVQVLM TLITSLTSAL TGTVTYEVLK PRLTELPLVQ
EFHFLLPLSV SVIILFQVYS MLVLGEIAPK TLAIRNNERI AALLSRPTLF LTETLSLPVR
MITATSQGLL RMLGVRNSRS AYPISPEELD LLLKEGTEQG VINRTEQDLI QSVFKFTDIS
VREVMVPRMK MVVMDASMTI EQATNFLSDH RFSRYPVVRT GTGEVVGILY YKDLFENYVR
SRQGRLTDLV HAPFFIPESM KVAHTLKEMQ KRRTQMALVL SEYGTLEGLV TMEDLLEELV
GEIEDESDDI QKPVERLRDG SYLVDASQSI RDLREDYHLD IPEGDDYETL AGFVVAQLQT
IPRGGEFFYM NHLKVTIVDM DKYRVSRVKI EPVPDMPDLP PAPARVSLPS STQKPFK
//
