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Database: UniProt
Entry: B2TUV7_SHIB3
LinkDB: B2TUV7_SHIB3
Original site: B2TUV7_SHIB3 
ID   B2TUV7_SHIB3            Unreviewed;       398 AA.
AC   B2TUV7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=HemY protein {ECO:0000313|EMBL:ACD07176.1};
GN   Name=hemY {ECO:0000313|EMBL:ACD07176.1};
GN   OrderedLocusNames=SbBS512_E4261 {ECO:0000313|EMBL:ACD07176.1};
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609 {ECO:0000313|EMBL:ACD07176.1, ECO:0000313|Proteomes:UP000001030};
RN   [1] {ECO:0000313|Proteomes:UP000001030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512 {ECO:0000313|Proteomes:UP000001030};
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) 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}.
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DR   EMBL; CP001063; ACD07176.1; -; Genomic_DNA.
DR   RefSeq; WP_000921791.1; NC_010658.1.
DR   AlphaFoldDB; B2TUV7; -.
DR   SMR; B2TUV7; -.
DR   STRING; 344609.SbBS512_E4261; -.
DR   GeneID; 75204792; -.
DR   KEGG; sbc:SbBS512_E4261; -.
DR   HOGENOM; CLU_037501_2_0_6; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000001030; 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; 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   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001030};
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   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
//
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