ID S6I1F6_9GAMM Unreviewed; 291 AA.
AC S6I1F6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase S54 rhomboid domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=OFPI_05820 {ECO:0000313|EMBL:EPJ54678.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ54678.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ54678.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family.
CC {ECO:0000256|ARBA:ARBA00009045}.
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:EPJ54678.1}.
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DR EMBL; ASZI01000039; EPJ54678.1; -; Genomic_DNA.
DR AlphaFoldDB; S6I1F6; -.
DR PATRIC; fig|1330035.3.peg.551; -.
DR Proteomes; UP000014830; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR Gene3D; 3.30.70.2080; -; 1.
DR Gene3D; 1.20.1540.10; Rhomboid-like; 1.
DR InterPro; IPR031976; NRho.
DR InterPro; IPR038244; NRho_sf.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR PANTHER; PTHR43731:SF26; RHOMBOID DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43731; RHOMBOID PROTEASE; 1.
DR Pfam; PF16733; NRho; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; Rhomboid-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000014830};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..57
FT /note="Rhomboid protease N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16733"
FT DOMAIN 137..278
FT /note="Peptidase S54 rhomboid"
FT /evidence="ECO:0000259|Pfam:PF01694"
SQ SEQUENCE 291 AA; 32265 MW; FDA158F78F05A1E0 CRC64;
MIVVFSAPLD VDLSGFTKQL WKMKIVHRVV IEQSQVLIVE DEHNAQLVTQ LYQHWQQEGE
LTPELVREVA QIGSNSATEN SRAVDFKKIP LVLLLLVSSL LLTLGIDFGQ NIELRKLLSI
TDFDYVGGYN SLNQSLESMQ LWRFISPIFM HFSIIHLIFN GLWIWVIGTV IEQQQKSLVL
LGIVIFSAIS SNIVQYLVSG PYFGGLSGVV YALISYAWLW DKMTEKKLLV VSNALMGFMV
VFLVLGYSGL LTRLGLGDIA NTAHLSGLVA GLIAAVVLAV VNVTSLKATD K
//
