ID A0A157SNC4_9BORD Unreviewed; 545 AA.
AC A0A157SNC4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Protoheme IX synthesis protein {ECO:0000313|EMBL:SAI71970.1};
GN Name=hemY {ECO:0000313|EMBL:SAI71970.1};
GN ORFNames=SAMEA3906486_03861 {ECO:0000313|EMBL:SAI71970.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI71970.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI71970.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI71970.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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; FKIF01000007; SAI71970.1; -; Genomic_DNA.
DR RefSeq; WP_066130524.1; NZ_FKIF01000007.1.
DR AlphaFoldDB; A0A157SNC4; -.
DR STRING; 288768.SAMEA3906486_03861; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000076848; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000076848};
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..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..133
FT /note="HemY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07219"
FT REGION 484..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 59217 MW; AE68A20B72FF0B92 CRC64;
MRTWLWTLLL AVVAVALAVM LRQHSGNVLL LIWPWRIEIS LTLAVLLLLA AFVALYVVLR
LLSWLLAIPD RVRAWRGRRA QARDHELLER GWIGMLEGRF AHAEKDLTRL FEQSKVRSRR
VLAALAAARS AHGLGEFDRR DRMIEAAREQ AGEDAGLQEA TATVAADMLL DQGKPQQALE
TLAPLQDGGA RHLHTSRLLL RAETALEHHE RVFTLARGLL RRNALDKAEG AQLIDHAGAA
RLRAGMAGDG WRVIWKDLKA EERLLPNIAL AGAAAFEADG EGAEAARILE AAIGDRFNPV
LVSAYARCDA SQVPRRLAKA ETWLAQRPAD TDLLTALGVL CLNGQLWGQA ERYLQRSLAR
RNDAQCHALL GSLYDRLDRP ADAARHWRLA TAARQALPVL ATDAALPAAD MGADPSHLDS
EGEYDALLPA SHATPVAAEP VPEHAPVADY VLDPDARELN ERPETIEAPA PVPQRSAIDI
EDYFDSAPIP PSAFEAPVSR YTPAAEPEPP AAATPPAKAQ PVPAQATPKP AAPLQSPDSP
SDNKG
//
