ID A0A0W0V2E6_9GAMM Unreviewed; 392 AA.
AC A0A0W0V2E6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Protoporphyrinogen oxidase {ECO:0000313|EMBL:KTD14255.1};
GN Name=hemY {ECO:0000313|EMBL:KTD14255.1};
GN ORFNames=Lisr_2483 {ECO:0000313|EMBL:KTD14255.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD14255.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD14255.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD14255.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KTD14255.1}.
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DR EMBL; LNYH01000149; KTD14255.1; -; Genomic_DNA.
DR RefSeq; WP_058502767.1; NZ_UGOE01000002.1.
DR AlphaFoldDB; A0A0W0V2E6; -.
DR STRING; 454.Lisr_2483; -.
DR PATRIC; fig|454.4.peg.2715; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000054761; Unassembled WGS sequence.
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 InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR Pfam; PF07219; HemY_N; 1.
DR Pfam; PF13181; TPR_8; 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:UP000054761};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..63
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 392 AA; 46097 MW; A923FF85C2AFBE01 CRC64;
MMRILFIFLL LFASGWLGVQ LSKDPGYIMI AIQHWTIETT LWIGVVAALL FFFLLYFLIH
LTVKLFNIPA RWRNWLNKRR IRKARATTSQ GLIEYSEGYW QKAKHHLIKA LPNTDTPLLN
YLTAARAAQK MGDNQLRDHY LREAQQSMPE AKIAVELTQA ELQLANQQWE QALATLKHLQ
DLAPSHPYVL KLLMNLYKEV RDWPQLISLL PELKKHQVIS QNEYEKLRLD VYYQEIKDRT
KSNHPQALEE FMKHLPKPLY FHPKLNAQYA RFLLQQNRHE QAEKVLRQCL RKEVYEELFV
LYGLCEQNTE QQLAFAESML KKAPHSATLY LCLGRLALKS QLWGKAKNYL QRSIELHPVP
ENHAELGKLY EQLNEPFKAS HCYKQGLELA IE
//
