ID M0CB24_9EURY Unreviewed; 342 AA.
AC M0CB24;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase A24B, FlaK domain protein {ECO:0000313|EMBL:ELZ19099.1};
GN ORFNames=C476_12888 {ECO:0000313|EMBL:ELZ19099.1};
OS Natrinema limicola JCM 13563.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ19099.1, ECO:0000313|Proteomes:UP000011615};
RN [1] {ECO:0000313|EMBL:ELZ19099.1, ECO:0000313|Proteomes:UP000011615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ19099.1,
RC ECO:0000313|Proteomes:UP000011615};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ19099.1}.
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DR EMBL; AOIT01000050; ELZ19099.1; -; Genomic_DNA.
DR RefSeq; WP_008013597.1; NZ_AOIT01000050.1.
DR AlphaFoldDB; M0CB24; -.
DR STRING; 1230457.C476_12888; -.
DR PATRIC; fig|1230457.4.peg.2590; -.
DR eggNOG; arCOG02298; Archaea.
DR OrthoDB; 19094at2157; -.
DR Proteomes; UP000011615; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1220; -; 1.
DR InterPro; IPR009655; Preflagellin_peptidase_C.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR PANTHER; PTHR36506; PREFLAGELLIN PEPTIDASE; 1.
DR PANTHER; PTHR36506:SF1; PREFLAGELLIN PEPTIDASE; 1.
DR Pfam; PF06847; Arc_PepC_II; 1.
DR Pfam; PF01478; Peptidase_A24; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011615};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..138
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
FT DOMAIN 307..336
FT /note="Preflagellin peptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06847"
FT REGION 218..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 36444 MW; 5E90E792A53BFA07 CRC64;
MTLAGAVATG PDLCRLLAVP VFTWVAYRDF ETRRVSSSVW IPLSLLGTVL LVWDGWLAWT
AGGTGWTYEF LVPTALSLGL VVPIAYLFWW VGGFGGADAK ALLVLAVLFP TFPEYALGSW
TVPLATPPLG AFSFTILTNA VLVGIALPLV LAVRNAVAGR IAPVMVVGWP VFWERIPETH
GRLLETPAGL TRSGLDLDAL RMYLRWRGLS LAELREQPEQ YRDPASLPAE PNPPTDGAVT
ADGGQRGDGG TLASDDDSAA AEAEDGSTTA IEHDDPWGAE AFLDDIEGSA YGTTPETLRD
GLEVLAREET VWVSPGTPFL VPVFVGLVVA LGYGDLLLGT LL
//
