ID D3HP37_LEGLN Unreviewed; 394 AA.
AC D3HP37;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Protoporphyrinogen IX and coproporphyrinogen III oxidase HemY {ECO:0000313|EMBL:CBJ10650.1};
GN Name=hemY {ECO:0000313|EMBL:CBJ10650.1};
GN OrderedLocusNames=LLO_0322 {ECO:0000313|EMBL:CBJ10650.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10650.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10650.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10650.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- FUNCTION: Involved in a late step of protoheme IX synthesis.
CC {ECO:0000256|ARBA:ARBA00002962}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004744}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; FN650140; CBJ10650.1; -; Genomic_DNA.
DR RefSeq; WP_003633305.1; NC_013861.1.
DR AlphaFoldDB; D3HP37; -.
DR STRING; 661367.LLO_0322; -.
DR KEGG; llo:LLO_0322; -.
DR eggNOG; COG3071; Bacteria.
DR HOGENOM; CLU_037501_2_1_6; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042168; P:heme metabolic process; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005254; Heme_biosyn_assoc_TPR_pro.
DR InterPro; IPR010817; HemY_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR Pfam; PF07219; HemY_N; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..132
FT /note="HemY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07219"
SQ SEQUENCE 394 AA; 45669 MW; F8DBC5CD957D66C6 CRC64;
MIRVLFAFLI LLAAVILGIQ LNKDPGYVLI AINHWTIETT VWVAIFTLIL LFMIVYLFLG
ICQKISLTPS KLTRWHARKR FRKAQAITRK GLIEYSEGNW VKAKNHLIQG LPNSDTPLLN
YLTAARAAQK MGDNQLRDDY LREAQQSMPE AKIAVELTQA ELQLSNHQWE QALATLKHLH
TIAPRHPYVL MLMMRLYQEI RDWPQLITLL PDLKKYKVIN QQEFEQIQYD TYLQRLRDLA
KQNQSSAVNS FFQSIPKTIV NNPEVIAEYT RFLLKNNEFT TAKNLVYRTL RKDFNPRLIE
LYAMLPADEH QLTFAESLLK KKPHSAALYL CLGQLCIKLQ LWGKAKYYLE KSNEIEPTPL
AYEAKGTLHE KLGEEALACN SYKKGIELIT KKII
//
