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Database: UniProt
Entry: S6GCM2_9GAMM
LinkDB: S6GCM2_9GAMM
Original site: S6GCM2_9GAMM 
ID   S6GCM2_9GAMM            Unreviewed;       440 AA.
AC   S6GCM2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=HemY N-terminal domain-containing protein {ECO:0000259|Pfam:PF07219};
GN   ORFNames=OFPII_38090 {ECO:0000313|EMBL:EPJ44010.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ44010.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ44010.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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:EPJ44010.1}.
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DR   EMBL; ASZJ01000180; EPJ44010.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6GCM2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000014822; 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   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:UP000014822};
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        43..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..133
FT                   /note="HemY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07219"
FT   REPEAT          370..403
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          400..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  48933 MW;  CBA606CBABD9BF12 CRC64;
     MKRVLILLFI VLAAGAFIGE KMVQDPGYVL LAFNNTTIET SVWVLLLLTF FGFLITHWTV
     NLFFRIGIPG QFIGRWRKAR IASSAQKRTF KGLIALSEGQ WWQAQRLLSQ TAPIAAQPLI
     NYLGAAKAAH EQGNTADTDE FFARARAIAP AAEVSISLQE VDVLMDRGNS AQALITLKRL
     HSLAPKHTGI LRHLAELHQN QQDWDGLIAL MSKLRKHKVF TIEQLAAMET NCYRQMLSTV
     VKKLPVECST DVRVKALTKG WKALPNTLNQ TAAMKATYAS ALNAANAPDD AEKFLRTQIK
     RDWDNQLIGL YGTLQTSDPT KHYNTVAGWL KKQPTHAALE LCAARLAMFN EKWQIAVQHY
     QSSIDLQPKV EAYRGLARLL ESLGEHEKSL EMNQKAMDLT EDDSPLIPLP APLETPAEET
     AKTAESTAIK VEKKPTTASA
//
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