ID C9Y4U9_CROTZ Unreviewed; 387 AA.
AC C9Y4U9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Protein hemY {ECO:0000313|EMBL:CBA27051.1};
DE EC=1.3.3.4 {ECO:0000313|EMBL:CBA27051.1};
GN Name=hemY {ECO:0000313|EMBL:CBA27051.1};
GN OrderedLocusNames=Ctu_02340 {ECO:0000313|EMBL:CBA27051.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA27051.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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; FN543093; CBA27051.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y4U9; -.
DR KEGG; ctu:CTU_02340; -.
DR PATRIC; fig|693216.3.peg.223; -.
DR HOGENOM; CLU_037501_2_0_6; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002069; Chromosome.
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; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR Pfam; PF07219; HemY_N; 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:CBA27051.1};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
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 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..121
FT /note="HemY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07219"
FT REPEAT 317..350
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 387 AA; 43908 MW; 0FE3CB7E6861C4C2 CRC64;
MAGIVVGPMV AGHQGYVLIQ TDTWNIETSV TGLAIMAILS LVVLFAIEWL LRRLFHTGAR
TRGWFAGRKR SRARKQTKLA LLKLAEGDYQ QVEKLMSKNA DHAEQPVVNY LLAAEAAQQR
GDEARANQHL ERAAELADND QIPVEITRVR LQLARNENHA ARHGVDRLLE ITPRHPEVLR
LAEQAYIRTG AWSSLLDIIP SMQKAGVGDD EHRDALTRQA WIGLMDQARA DQGSDGLKTW
WRNQSRKTRH QPALQVAMAE HLIECDDHQT AQEIILDGLK RQYDDRLVLL MPRLKAGNPE
QLEKALRQQI KTYGDRPLLW STLGQLLMSH GEWKEASLAF RAALKQRPDA FDYAWLADVL
DRLHQPEEAA TMRRDGLLLT LQQNTPQ
//
