ID A0A0Q4N868_9GAMM Unreviewed; 396 AA.
AC A0A0Q4N868;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Protoheme IX biogenesis protein {ECO:0000313|EMBL:KQN60287.1};
DE EC=1.3.3.4 {ECO:0000313|EMBL:KQN60287.1};
GN ORFNames=ASF13_22390 {ECO:0000313|EMBL:KQN60287.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN60287.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN60287.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN60287.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN60287.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN60287.1,
RC ECO:0000313|Proteomes:UP000050856};
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 -!- 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:KQN60287.1}.
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DR EMBL; LMLK01000008; KQN60287.1; -; Genomic_DNA.
DR RefSeq; WP_056234740.1; NZ_LMLK01000008.1.
DR AlphaFoldDB; A0A0Q4N868; -.
DR STRING; 1736225.ASF13_22390; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000050856; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
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; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR Pfam; PF07219; HemY_N; 1.
DR Pfam; PF07719; TPR_2; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
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 Oxidoreductase {ECO:0000313|EMBL:KQN60287.1};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
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"
FT REPEAT 328..361
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 396 AA; 44902 MW; 32F3F79E0CB39C4B CRC64;
MLKVLLLFLL LIAGVVLGPM IAGHQGYVLI QTDSWNIETS VTGLAIVLIL SLLVILGVEW
LLRRLFHTGA RTRGWFTGRK RRSARRQTHA ALVKLAEGDH QQVEKLLSRH ADHADQPMVN
YLLAAEAAQQ RGDEKRADQH LARATELNDG DPLPVEITRV RIQLARGEDH AARHGIDRLL
EIAPRHPELL RLAEQAYIRT GAWSALLDIL PAMEKIRLGD EAHRLALQQQ AWLGLMNQAM
ADQGSEGLKR WWQQQSRKTR HEIPLQVAMA DHLIVCDDHD TAQQIVLDGL KRQYDERLVL
LMPRLKGGNP ERLEKALRQQ IKQHGATPLL HSTLGQLLMQ HGEWQQASEA FRAALQQRPD
AFDYAWLADT LDRQHKPEEA AQMRRDGLLL TLKNNA
//