ID I3UBN0_ADVKW Unreviewed; 475 AA.
AC I3UBN0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=HemY, N-terminal domain-containing protein {ECO:0000313|EMBL:AFK62418.1};
GN OrderedLocusNames=TKWG_10900 {ECO:0000313|EMBL:AFK62418.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62418.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK62418.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
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; CP003555; AFK62418.1; -; Genomic_DNA.
DR RefSeq; WP_014750509.1; NC_017964.1.
DR AlphaFoldDB; I3UBN0; -.
DR STRING; 1036672.TKWG_10900; -.
DR KEGG; aka:TKWG_10900; -.
DR HOGENOM; CLU_037501_0_0_4; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000005267; Chromosome.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..134
FT /note="HemY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07219"
FT REGION 408..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52837 MW; AA2F93F99F7F907B CRC64;
MRTSLKLLVL FAVAVAAALL LRDSSGYFMV VTGDERRTVS LAAGLVFIVI AFFVFYLIFR
FIGVLMDAPT RWRDWNQRRH TRKDYDLLER GWVELLEGRS SPAEKDLTRL LNRSRDSGRQ
ALASLAAAKA AHNQSRYAER DALLLTAQAK AQGNPRMQDA ATTIRAEMLL EQGESKQALA
LLEPLAKAGG ANQDHIQKLL LRGYKQIGNQ DKLLQVARAL NKKGTIDSFE GQRLIEHAGA
AVMKATTRDS WTNTWKSFSA SEKAMPLIAL AAAEKAQAAG QSDTAGQILE ASLREHIDAR
LLNAYVQCPA EQVNARLTKA QQWLEKDENN PDLLNALGFL CLAAQLWGQA ERYLTRSLKL
REDPRTHTLL GALYDRLGKP AEAVKHWRFA SASISMLPTV AGEKYLPAAD TRMDPDGPPD
RKRADQQIEQ EHADEASEKT IYAKRPEADD EYFDSAPIPG IGADELNENR NHEKP
//
