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Database: UniProt
Entry: A0A3L8PYB3_9GAMM
LinkDB: A0A3L8PYB3_9GAMM
Original site: A0A3L8PYB3_9GAMM 
ID   A0A3L8PYB3_9GAMM        Unreviewed;       386 AA.
AC   A0A3L8PYB3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Heme biosynthesis protein HemY {ECO:0000313|EMBL:RLV60290.1};
GN   ORFNames=D5018_07805 {ECO:0000313|EMBL:RLV60290.1};
OS   Parashewanella curva.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Parashewanella.
OX   NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV60290.1, ECO:0000313|Proteomes:UP000281474};
RN   [1] {ECO:0000313|EMBL:RLV60290.1, ECO:0000313|Proteomes:UP000281474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C51 {ECO:0000313|EMBL:RLV60290.1,
RC   ECO:0000313|Proteomes:UP000281474};
RA   Wang G.;
RT   "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT   Pseudoshewanella and Parashewanella.";
RL   Submitted (SEP-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV60290.1}.
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DR   EMBL; QZEI01000018; RLV60290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8PYB3; -.
DR   OrthoDB; 7067577at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000281474; 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; 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   Pfam; PF13181; TPR_8; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50293; TPR_REGION; 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:UP000281474};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..70
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   386 AA;  43911 MW;  978ACE70E8B781C8 CRC64;
     MIRTLAYIVI ILLGLVLSPW ILSHTGYLYL SIGDYEVETS VVFAVVALLV IFSAIQLIEW
     LFVGLINIFV RRGWLSSRWR RQSARKHTLQ GALAIAEEDW VNAEKSMCKG ASNGELPLVN
     WLAAARAAHH QGSTEQRDHY LNQAEKLADN KLSIATTRVR YLIQQGELET ARVQLDKLIA
     ANSNKPALIK LGLELYHLQQ DWSAIKLLLP KVTKLKLLNQ SELEELQQQV NRALLKQVEH
     KPELEKVWHW LSRKERKTSA NLAEYAISLA RLGDTIEAKK IIYKAIKSHP VNEFFDLLPS
     IVNAGDDDIR KLLAGLESSQ DNNASYHRCL AKLNQQTNNF SEAKHHWQRV IELQPSVSSW
     TALGKLHEQL GEQAKALNCY RHALQF
//
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