ID A0A1I1T6H9_9BACI Unreviewed; 519 AA.
AC A0A1I1T6H9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Rhomboid family peptidase. Serine peptidase. MEROPS family S54 {ECO:0000313|EMBL:SFD54202.1};
GN ORFNames=SAMN05216238_102135 {ECO:0000313|EMBL:SFD54202.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD54202.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFD54202.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD54202.1,
RC ECO:0000313|Proteomes:UP000199474};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOMR01000002; SFD54202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1T6H9; -.
DR STRING; 640948.SAMN05216238_102135; -.
DR OrthoDB; 9813074at2; -.
DR Proteomes; UP000199474; 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; 1.20.1540.10; Rhomboid-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43731:SF26; RHOMBOID DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43731; RHOMBOID PROTEASE; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF144091; Rhomboid-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 184..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..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 320..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..362
FT /note="Peptidase S54 rhomboid"
FT /evidence="ECO:0000259|Pfam:PF01694"
FT REPEAT 470..503
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 519 AA; 58990 MW; 20D538D5E6BCA313 CRC64;
MYLDESYTMY KLAWHLIEHD KFELVHINEN GELWLEKFEG KTSRVARLFH GGFDWKNHMK
KDIGQTFQKA KAMKRYFRSK HIEVHNVYID SHTPIDDWEI LKKKMQLNEK NPISMKVYYL
SDKDREEELN RFLTAIGGTF EPAEQSADNA EKEEEVNQIR EKLTGKIKQK ENEIKDIFSY
GKPLLTYILL AVNILLFFLL EMNGDSTSPA RLIEFGAKYN PAIIEDGEWW RIISSMFLHI
GIAHILLNML AVYYLGTAVE RIYGSLRFIV IYFMAGIGGG LASFAFTTNV SAGASGALFG
LFGALLFFGC IHRRIFFQTM GMNLLIVIGI NIVFGLSVPQ VDNGAHMGGL ISGFVASAVL
YLPKKKNLII QTAAFIVYSL LIVGLAVYGV QHNESSAEYQ LMKAEQLIAE EQYERVIAVV
TEGLQLSDGS ESDLKSHLLF QRAYSQIRLE NTEEAIADLE ISVELNSSLA EAHYNLAVLY
SDNNDSTNAE EHIEKAYELN PQNEDFHELY EHITGNKPN
//