ID A0A0N0GMV8_9NEIS Unreviewed; 398 AA.
AC A0A0N0GMV8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative protoheme IX biogenesis protein {ECO:0000313|EMBL:KPC52032.1};
GN ORFNames=WG78_13270 {ECO:0000313|EMBL:KPC52032.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC52032.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC52032.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC52032.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-2015) 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:KPC52032.1}.
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DR EMBL; LAQT01000010; KPC52032.1; -; Genomic_DNA.
DR RefSeq; WP_053938305.1; NZ_LAQT01000010.1.
DR AlphaFoldDB; A0A0N0GMV8; -.
DR STRING; 857265.WG78_13270; -.
DR OrthoDB; 7053339at2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000037939; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000037939};
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..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..134
FT /note="HemY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07219"
SQ SEQUENCE 398 AA; 44712 MW; 359B1703F331645F CRC64;
MKILIWLVAL FALAVGVTLF AQLNTGYALL FVPPWRIEIS INVFILLVVL TVVIVYAITR
VVAELGGLPT RVRKYRERQR LDASIKLERE ARIAFFEGRY QRAERLAAEA LALSTAQEAI
AVNGLLAARA AHAMRDFARR DKHFADLKQK LGGPQKLALA MNMAELYLDE RRYADADVAI
AEARAISPKL TAAMRLELRL RQREDDPQAV LQLVDQLSRS EALDAAQASR IRIQAQLSLL
ASVPMSLAEL KVWWSKLSAD DKQAPAIVLA MVDQLVAHDA PEDARRIIEE ALALQWSPEL
VERYGRLHLP AEARVQQLQL AETWLHTRPN DYQLLLTLGR LCHARSLWGK AQNYLEACLA
VEKTALAHAE LASLLEQLDR HEEAARHYRA SLELALGR
//
