ID A0A0W1ADC1_9GAMM Unreviewed; 393 AA.
AC A0A0W1ADC1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Protoporphyrinogen oxidase {ECO:0000313|EMBL:KTD79340.1};
GN Name=hemY {ECO:0000313|EMBL:KTD79340.1};
GN ORFNames=Lwal_1412 {ECO:0000313|EMBL:KTD79340.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD79340.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD79340.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD79340.1,
RC ECO:0000313|Proteomes:UP000054729};
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:KTD79340.1}.
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DR EMBL; LNZB01000036; KTD79340.1; -; Genomic_DNA.
DR RefSeq; WP_058480114.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1ADC1; -.
DR STRING; 66969.Lwal_1412; -.
DR PATRIC; fig|66969.6.peg.1547; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000054729; 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 SMART; SM00028; TPR; 4.
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:UP000054729};
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..59
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 393 AA; 44903 MW; 9D0FB215F9985DC8 CRC64;
MFRILLAFFI LLTSVVLGTQ LNLDPGYVLI AINHWTLETT LWTALIGLLL LFIVSHLMIQ
LCHRIAKTPA TINKWHSRRL AHKAQVITRK GLIEYSEGYW QKAKNHLIQA LPNTDTPLLN
YLTAARAAQK MGDSTLRDHY LREAQQCMPE AKIAVELTQA QLQIANHQWE QALATLKHLQ
DLAPRHPYVL KLLMNLYIEI KDWHQLIALL PDLKKNSVIS NQEFSQLQEN TYLQAMNELI
KQNQLSQVHT VFNSLPKALN GNSAIIAEYV RFLIKLGEFT QAEQLIKQNL RKEVDNQLIE
LYGLLPATEQ QLAFAESLLK KNPHSAALYL CLGRICIYQH LWGKAKHYIE QSIALNPTPA
AYNELGKLHE KLNDPLSSCV CYKKGLQLVT ETD
//