Y405_HALVD
ID Y405_HALVD Reviewed; 657 AA.
AC D4H031;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Probable cell surface fusion protein HVO_0405 {ECO:0000305};
DE Contains:
DE RecName: Full=LVIVD repeat domain-containing protein {ECO:0000305};
DE Contains:
DE RecName: Full=NifU-like domain-containing protein {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=HVO_0405 {ECO:0000312|EMBL:ADE02310.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, EXPORT VIA THE
RP TAT-SYSTEM, DOMAIN, PROTEOLYTIC PROCESSING, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 3-ARG-ARG-4.
RC STRAIN=H53;
RX PubMed=28069824; DOI=10.1128/jb.00802-16;
RA Abdul Halim M.F., Stoltzfus J.D., Schulze S., Hippler M., Pohlschroder M.;
RT "ArtA-dependent processing of a Tat substrate containing a conserved
RT tripartite structure that is not localized at the C terminus.";
RL J. Bacteriol. 199:E00802-E00802(2017).
CC -!- SUBCELLULAR LOCATION: [LVIVD repeat domain-containing protein]:
CC Secreted {ECO:0000269|PubMed:28069824}. Cell surface
CC {ECO:0000305|PubMed:28069824}. Cell membrane
CC {ECO:0000269|PubMed:28069824}. Note=The processed N-terminal portion
CC localizes to the membrane fraction and is probably membrane anchored
CC via lipidation. {ECO:0000269|PubMed:28069824}.
CC -!- SUBCELLULAR LOCATION: [NifU-like domain-containing protein]: Cell
CC membrane {ECO:0000269|PubMed:28069824}. Note=The C-terminal fragment
CC localizes to the membrane, likely due to the hydrophobic region that is
CC part of the tripartite structure. However, the C-terminal fragment is
CC present in much lower abundance that the full-length protein, possibly
CC due to the degradation of this C-terminal region.
CC {ECO:0000269|PubMed:28069824}.
CC -!- DOMAIN: The N-terminal region contains several LVIVD repeat domains,
CC which are often found in proteins that localize to the cell surface.
CC The C-terminal region contains a NifU-like domain, originally
CC discovered in proteins involved in nitrogen fixation.
CC {ECO:0000305|PubMed:28069824}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. {ECO:0000255|PROSITE-
CC ProRule:PRU00648, ECO:0000269|PubMed:28069824}.
CC -!- PTM: Cleaved near the Pro-Gly-Phe (PGF) motif by the archaeosortase
CC ArtA, which recognizes a tripartite structure consisting of a conserved
CC PGF motif, followed by a transmembrane alpha helix domain and a cluster
CC of basic residues. {ECO:0000269|PubMed:28069824}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not result in any
CC discernible surface adhesion phenotype under standard conditions and
CC mutant does not exhibit a discernible growth defect.
CC {ECO:0000269|PubMed:28069824}.
CC -!- MISCELLANEOUS: HVO_0405 may be the result of a fusion of two genes, one
CC encoding an ArtA substrate and the second encoding a protein containing
CC a NifU-like domain. As a result of the fusion, the tripartite structure
CC recognized by ArtA is closer to the center of the protein than to the
CC C-terminus. However, despite this atypical localization of the PGF
CC motif, HVO_0405 is indeed processed by ArtA.
CC {ECO:0000305|PubMed:28069824}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NfuA family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE02310.1; -; Genomic_DNA.
DR RefSeq; WP_004044519.1; NZ_AOHU01000102.1.
DR AlphaFoldDB; D4H031; -.
DR SMR; D4H031; -.
DR STRING; 309800.C498_16678; -.
DR EnsemblBacteria; ADE02310; ADE02310; HVO_0405.
DR GeneID; 8924101; -.
DR KEGG; hvo:HVO_0405; -.
DR PATRIC; fig|309800.29.peg.3231; -.
DR eggNOG; arCOG02565; Archaea.
DR eggNOG; arCOG03027; Archaea.
DR HOGENOM; CLU_027478_0_0_2; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR013211; LVIVD.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF08309; LVIVD; 2.
DR Pfam; PF01106; NifU; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 31..?
FT /note="LVIVD repeat domain-containing protein"
FT /id="PRO_0000444158"
FT CHAIN ?..657
FT /note="NifU-like domain-containing protein"
FT /id="PRO_0000444159"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 51..85
FT /note="LVIVD repeat 1"
FT /evidence="ECO:0000305|PubMed:28069824"
FT REPEAT 99..141
FT /note="LVIVD repeat 2"
FT /evidence="ECO:0000305|PubMed:28069824"
FT REPEAT 148..187
FT /note="LVIVD repeat 3"
FT /evidence="ECO:0000305|PubMed:28069824"
FT REPEAT 246..322
FT /note="LVIVD repeat 4"
FT /evidence="ECO:0000305|PubMed:28069824"
FT REPEAT 340..372
FT /note="LVIVD repeat 5"
FT /evidence="ECO:0000305|PubMed:28069824"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..625
FT /note="NifU-like"
FT /evidence="ECO:0000305"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..470
FT /note="PGF sorting signal"
FT /evidence="ECO:0000305|PubMed:28069824"
FT COMPBIAS 443..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 3..4
FT /note="RR->KK: Prevents ArtA-dependent processing."
FT /evidence="ECO:0000269|PubMed:28069824"
SQ SEQUENCE 657 AA; 69804 MW; 6B5BCB8A308195F2 CRC64;
MDRRQFLRTV GASALAVSTA AVVGSRPATA HPGPFEPLGR IDIDGAKEAV VSADGETVFV
AATSGYAVVD ISAPERQELL AERRDPLSDR EDGPFRGLYD AKLDGDTLLV VGPANPIPGA
PAGVLVVDVS DPATPEEIAF HETEFPIHNC FAADGRAYLT ANDGDRNPLV VLDIDSGDEL
GRWSVVDADD RWADVPPSMR SVHDVWVHDR VAHVALWDAG TWLVDLSDPA SPWVLGAVSP
GDPEEIAALT PRGRNRERRT PPGNHHYVAT DDAGDLLGVG VESWAIEVDR DDGTTELVGG
PSGVELWDVT DPANPERRST IEPPASPDPT LGGVWTTAHN FDFRDDRLYT SWYRGGVKRH
DVSDPTDPVE LAWWRDPERA SFWTAQYAYP FADEGVFVAS SRGVGDASPA LYTFPDHAGD
QRDPPTLRAE PTTEPLVNTP TPTPSPSGNE TAASASETES STSTTDAPGF GLGVGAAALG
VAGWLVRVTS GATESDRRSR PRASTGTPHR VVPASNLSRT TEIAFLSPAG ASGEPFHSNP
WGSKHRSMSD ESESLKERVE TWMVGQMPII QMHGGNSVVR KADAESGEVV VELGGACAGC
GISNITAQNI QSDLIMTFDE ITDVQVKVPS SGDHGSSTVE GGRGGELQYG DEGPGHF
