ID A0A1F4HP29_9BURK Unreviewed; 736 AA.
AC A0A1F4HP29;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGA99718.1};
GN ORFNames=A3E25_19045 {ECO:0000313|EMBL:OGA99718.1};
OS Burkholderiales bacterium RIFCSPHIGHO2_12_FULL_69_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797561 {ECO:0000313|EMBL:OGA99718.1, ECO:0000313|Proteomes:UP000177017};
RN [1] {ECO:0000313|EMBL:OGA99718.1, ECO:0000313|Proteomes:UP000177017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:OGA99718.1}.
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DR EMBL; MESD01000126; OGA99718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4HP29; -.
DR Proteomes; UP000177017; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..309
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 472..518
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 510..555
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 736 AA; 80858 MW; 3DD2B03C096A801F CRC64;
MQTLLSEHWH AVRFLKPRLR PGVQPLHRVL RGQPWVLLQD PVTQRFHRVS PPVWRVLVLL
DGSRTLDEVW AESLAQGEAA ASGEAPAGDA ISQHELVQLL SSLHANDLIA TQVSPDAGEV
FERYQRQRRA KLKQSWLNPM SIKLPLLHPD AWFQRQAALA RAVFTLPMLL LWALLVAPAV
GLAWQHWTPL TENLSDRVLS AGNLALLWAV YPAVKAVHEW AHGLAIKAWG GTVREIGLMF
IVLTPVPYVD ATSSYRFPSK WARAAVAAAG IMAELVLGAL ALYIWLLAEP GWVRALAFNV
VLIAGVSTVL VNGNPLMRYD GYFIACDLLE TPNLAQRSTQ FWAWLVDRYG FGAREAPAPQ
ATRGERWLMG LYGLVAPVYR LAITVGLIWF VASEYRLLGA VMALMAAWAA LVMPLWKGWQ
HLRQSPALVQ RRDVALRRTM LAVVALLAGL LLLPLPFYSV HQAVVWLPDE ALVRADSAGQ
VVRPLVASGD AVQRGQPLLL LDNPALDSEL ASAEAAVAQT DAQLRRAEID EPVQLAALRA
ELASRAQRLA EAQRRVAALR VDAGAVGRWM PAAPTELAGR YVRRGEVVGH VVAGPSRWLR
CAVTQEDLDL IRRGHGEGDS GRAAAAGLPA VQVRLAQRPR ELHHARVTRQ VPGGEFDLVS
PALGSSGGGE IAVDPAVSEG TRSLRRIFDI ELQLDEAAAQ PVFGDRAWVR FDLGATPLGW
QWALRLRQLF LARLNV
//
