ID B4F1X0_PROMH Unreviewed; 409 AA.
AC B4F1X0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Porphyrin biosynthesis protein {ECO:0000313|EMBL:CAR46529.1};
GN Name=hemY {ECO:0000313|EMBL:CAR46529.1};
GN OrderedLocusNames=PMI3329 {ECO:0000313|EMBL:CAR46529.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR46529.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR46529.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR46529.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR46529.1; -; Genomic_DNA.
DR RefSeq; WP_004246334.1; NC_010554.1.
DR AlphaFoldDB; B4F1X0; -.
DR EnsemblBacteria; CAR46529; CAR46529; PMI3329.
DR GeneID; 6802306; -.
DR KEGG; pmr:PMI3329; -.
DR eggNOG; COG3071; Bacteria.
DR HOGENOM; CLU_037501_2_0_6; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000008319; Chromosome.
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; 1.
DR InterPro; IPR005254; Heme_biosyn_assoc_TPR_pro.
DR InterPro; IPR010817; HemY_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR Pfam; PF07219; HemY_N; 1.
DR SUPFAM; SSF48452; TPR-like; 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 Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
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..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"
SQ SEQUENCE 409 AA; 46685 MW; 8ABD690F6E5A43F4 CRC64;
MFKILLLFVV LIAGIIFGPV LAGHQGYVFI QTDNWDIETS VTSLVIMFVL LQLILLLLGW
CYRRFIGTGS KAYSWFSLRK RSRARKQTRL ALMKLAEGDF KQVEKLMSRN ADYAEQPVVN
YLLAAEAAQQ RGDEFRVQQH LERASELADT NQLPVDITRV RILLAQNENH AARTGVDELL
NQVPRHPEVL RLAETAYIRT EAWQALLDII PSMQKIALHT DDELEQLRQQ AYIGLMGQKM
SENGCDGLKN WWKAQPRKIQ HDNGLRFVLA EHLIECNDPQ TAQTIILDGI KRHYDERLIL
LLPRLKNSDP DSILKVLNSL IKQHGPTPLL NSTVGQIAMQ QGQWAQAETA FRNALKQRPD
VHDFAWLADV LDKQNKSVES AKVRKDALLM TLKKDSVIFD EPKTNKALQ
//
