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Database: UniProt
Entry: A0A432W3C8_9GAMM
LinkDB: A0A432W3C8_9GAMM
Original site: A0A432W3C8_9GAMM 
ID   A0A432W3C8_9GAMM        Unreviewed;       392 AA.
AC   A0A432W3C8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=HemY N-terminal domain-containing protein {ECO:0000259|Pfam:PF07219};
GN   ORFNames=CWE09_11805 {ECO:0000313|EMBL:RUO23832.1};
OS   Aliidiomarina minuta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=880057 {ECO:0000313|EMBL:RUO23832.1, ECO:0000313|Proteomes:UP000288293};
RN   [1] {ECO:0000313|EMBL:RUO23832.1, ECO:0000313|Proteomes:UP000288293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLST1 {ECO:0000313|EMBL:RUO23832.1,
RC   ECO:0000313|Proteomes:UP000288293};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO23832.1}.
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DR   EMBL; PIPL01000003; RUO23832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432W3C8; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000288293; 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   InterPro; IPR019734; TPR_repeat.
DR   NCBIfam; TIGR00540; TPR_hemY_coli; 1.
DR   Pfam; PF07219; HemY_N; 1.
DR   SMART; SM00028; TPR; 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:UP000288293};
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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..138
FT                   /note="HemY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07219"
FT   REPEAT          331..364
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   392 AA;  44507 MW;  836A8CD4EE59954A CRC64;
     MARGVRLVFK ALLLLLIIVA GFIVGPLWSG QTGYVMIAVS GYTVETSLVV LAMAVILLLL
     VFWLIEWLLR KILAGSRLSS SWLQRRRLKK GDTQLSSAFN SWLTHDYAKA QEQAEQATSN
     LKRPQQAYLL AAMAANARHD SVSYQRLLEK ANSAEDDKQL PLLLAEAESA APKEAQQQLQ
     HLLKQYPRHP GVLRVAAKTF YRHQQWSELR PLLPELAKKN LIEPRLLLSY TQKSYQAYFA
     VAQEDPTELH KRWRDLDRQL RQDTSVRLEY IRALLDNQQQ EEAAKVAIKG LRKGYLEPID
     LLLGQSQFDW QGSALLTEHI QQMVKKQPDD ANALALLGLL AMQQNDHDLA ERALRKALEL
     YPNKRFYQLL GDTYLAAEQS AKALAAYKAA SQ
//
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