HEMY_ECOL6
ID HEMY_ECOL6 Reviewed; 398 AA.
AC P0ACB8; P09128;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein HemY;
GN Name=hemY; OrderedLocusNames=c4721;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Involved in a late step of protoheme IX synthesis.
CC {ECO:0000250}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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DR EMBL; AE014075; AAN83154.1; -; Genomic_DNA.
DR RefSeq; WP_000921791.1; NC_004431.1.
DR AlphaFoldDB; P0ACB8; -.
DR SMR; P0ACB8; -.
DR STRING; 199310.c4721; -.
DR EnsemblBacteria; AAN83154; AAN83154; c4721.
DR GeneID; 66672294; -.
DR KEGG; ecc:c4721; -.
DR eggNOG; COG3071; Bacteria.
DR HOGENOM; CLU_037501_2_0_6; -.
DR OMA; WGKARDY; -.
DR BioCyc; ECOL199310:C4721-MON; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF07219; HemY_N; 1.
DR Pfam; PF07719; TPR_2; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00540; TPR_hemY_coli; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Porphyrin biosynthesis;
KW Repeat; TPR repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Protein HemY"
FT /id="PRO_0000135277"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..39
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 118..151
FT /note="TPR 1"
FT REPEAT 328..361
FT /note="TPR 2"
SQ SEQUENCE 398 AA; 45245 MW; 56BDDC4E19099D3C CRC64;
MLKVLLLFVL LIAGIVVGPM IAGHQGYVLI QTDNYNIETS VTGLAIILIL AMVVLFAIEW
LLRRIFRTGA HTRGWFVGRK RRRARKQTEQ ALLKLAEGDY QQVEKLMAKN ADHAEQPVVN
YLLAAEAAQQ RGDEARANQH LERAAELAGN DTIPVEITRV RLQLARNENH AARHGVDKLL
EVTPRHPEVL RLAEQAYIRT GAWSSLLDII PSMAKAHVGD EEHRAMLEQQ AWIGLMDQAR
ADNGSEGLRN WWKNQSRKTR HQVALQVAMA EHLIECDDHD TAQQIIIDGL KRQYDDRLLL
PIPRLKTNNP EQLEKVLRQQ IKNVGDRPLL WSTLGQSLMK HGEWQEASLA FRAALKQRPD
AYDYAWLADA LDRLHKPEEA AAMRRDGLML TLQNNPPQ
