ID G6EZM6_9PROT Unreviewed; 595 AA.
AC G6EZM6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=CIN_08960 {ECO:0000313|EMBL:EHD14964.1};
OS Commensalibacter intestini A911.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14964.1, ECO:0000313|Proteomes:UP000005939};
RN [1] {ECO:0000313|EMBL:EHD14964.1, ECO:0000313|Proteomes:UP000005939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A911 {ECO:0000313|EMBL:EHD14964.1,
RC ECO:0000313|Proteomes:UP000005939};
RA Lee W.-J., Kim E.-K.;
RT "Genome Sequence of Commensalibacter intestini A911, isolated from
RT Drosophila gut.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:EHD14964.1}.
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DR EMBL; AGFR01000003; EHD14964.1; -; Genomic_DNA.
DR RefSeq; WP_008853886.1; NZ_AGFR01000003.1.
DR AlphaFoldDB; G6EZM6; -.
DR STRING; 1088868.CIN_08960; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000005939; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 147..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 63358 MW; 1780F7B9D9397C5A CRC64;
MALYLLGKTG FHSSEDFVIN GCSIYEQYGQ LTQILQKHCP SIYLAEPTIT DNKDPESSFI
SWYADTKTEP TIPLDSQQSL IDQKLADAVT SLSQAYPAGS AESTLLNAAL HVQNKQDILI
ADDKIVLKGW GVNASSGNDA SGLSLFPLSP VTPETSNDQN SDPVSNSAQL SATNTIIPPT
TGNIMNAPKR SMGGMPVFLT RLVAAILFFI IGLLLGWRIL YAERPTKIAK VPVMEAQDLV
RKKPEIDQKN KVLEDEIKKL EDLLKNPPCD LGKNRGAPEL NKSLDNSSAP MKSDGKNFQG
SLPDLLEKST VFILVKTKDD NGEDAIAAGS GFFVTPDTIV TNRHVVEGSD GTVLVTNKTL
GQFKKAHVVS ISSPSSDVNS FDLAVLKVED APPQQPLSFS LEAQPLQTVV AAGYPGIIIR
QDGALKRLAQ GDVNAIPGVI LTKGEINAIQ ENSKGEKIMP HSAAVSPGNS GGELVDLCGR
VVGVNTFVTM DSETSSHSNY AQKSDSIVKA LQGANIPIQV QSGACKDGIP TGNVDGDKQP
AAAPNTTPTK DDKTQGSQST PDQKADATKP KEDTKQPATT EQKTEQSSTS QGDKP
//
