ID A0A0Q4FUR7_9BURK Unreviewed; 435 AA.
AC A0A0Q4FUR7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Hemolysin {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASE76_12530 {ECO:0000313|EMBL:KQM69059.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM69059.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM69059.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM69059.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM69059.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM69059.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM69059.1}.
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DR EMBL; LMKO01000025; KQM69059.1; -; Genomic_DNA.
DR RefSeq; WP_055842294.1; NZ_LMKO01000025.1.
DR AlphaFoldDB; A0A0Q4FUR7; -.
DR STRING; 1735686.ASE76_12530; -.
DR OrthoDB; 9797674at2; -.
DR Proteomes; UP000051325; 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:SF5; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 1.
DR Pfam; PF00571; CBS; 1.
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; 1.
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:UP000051325};
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..196
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 279..341
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 435 AA; 46792 MW; E8A8CD4C5266287B CRC64;
MDFLLIALLT LLNGVFAMSE LALASSRRAR LIALAESGDK GASAALALLD NPTQFLSSVQ
VGITSIGMLN GILGEAAFSD DVAVLLQTVG APARAAEIGA TAIVVTIITF ITIVFGELVP
KRIGQLYPEK VALWVSRPMT WVATIAKPFV HLLSFSTHAV LKLLRVDNAA ERPVTEAEIV
ASLEEGVDAG IIEHQEHRMV QNVFHLDDRP LTSLMVPRAD IEWLPAMATV RDALEHAVKG
GDRGSHSWYP VCRGSLDDVV GIVSLSHLLA LEADSAGPIE SYVLPASFLP ETLSGMELLE
QFRAQSGRMV FVVDEYGVVQ GLMTPRDLLE AITGELQPGA EAQAWATQRG DGSWLLDGLM
PIGELKARLD IRDLPGEDRN LYNTLAGLLM SESGRLPVTG EQIECAGWIF EVVDLDGKRI
DKVMAMLPPE SATTG
//
