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Database: UniProt
Entry: A0A1R1MGU4_9GAMM
LinkDB: A0A1R1MGU4_9GAMM
Original site: A0A1R1MGU4_9GAMM 
ID   A0A1R1MGU4_9GAMM        Unreviewed;       415 AA.
AC   A0A1R1MGU4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=HemY N-terminal domain-containing protein {ECO:0000259|Pfam:PF07219};
GN   ORFNames=BGP75_04435 {ECO:0000313|EMBL:OMH38979.1};
OS   Motiliproteus sp. MSK22-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Motiliproteus.
OX   NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH38979.1, ECO:0000313|Proteomes:UP000187359};
RN   [1] {ECO:0000313|EMBL:OMH38979.1, ECO:0000313|Proteomes:UP000187359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH38979.1,
RC   ECO:0000313|Proteomes:UP000187359};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL   Submitted (AUG-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}.
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:OMH38979.1}.
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DR   EMBL; MIEQ01000022; OMH38979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1MGU4; -.
DR   STRING; 1897630.BGP75_04435; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000187359; 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:UP000187359};
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        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..134
FT                   /note="HemY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07219"
FT   REPEAT          338..371
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   415 AA;  47002 MW;  EB0D91E2091442F5 CRC64;
     MMKLLYVIGL ILLLVGTVVG ELIIKDPGYV LLSYQNTTIE TSIWGLVIVA TVLFVTLHLA
     IRFLQYVLER RRKINDWNNN RTRVRANRRT LNGLLALSSG DWQKAQRLLV SAADKAETPL
     INYLAAARAA HEEGLPDASD RYLEQAQKVM PKAETAIGIT RAQIQLSRGQ LEPCLATLKR
     LRGIAPRHTF VLKMLKQVYL QQQDWVSLSE LIPYLQKNDV LKGQQLRELE RKAYIGLMKE
     TLDQLPAESD APARIKALNK TWKSLPRELM NDSDLIASYV SLLAQNGSED KAETFLSDAI
     YREWDDSLVK LYGQIASSNP AKQLSTAKTW VHEHSDNATL QLTLGRLSLL NAQWEQAREH
     FEKSIELHNS QETYNELARL LKHLDDTEGF QKLMKDNLDS VTESLPKLPL PAGNT
//
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