ID E8RQ49_ASTEC Unreviewed; 570 AA.
AC E8RQ49;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADU12106.1};
GN OrderedLocusNames=Astex_0411 {ECO:0000313|EMBL:ADU12106.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU12106.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002395; ADU12106.1; -; Genomic_DNA.
DR AlphaFoldDB; E8RQ49; -.
DR STRING; 573065.Astex_0411; -.
DR KEGG; aex:Astex_0411; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_512712_0_0_5; -.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000001492; Chromosome 1.
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; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF68; SERINE PROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..570
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005674805"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 348..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 61444 MW; E1BD55A682565DD8 CRC64;
MLAAGIVALT MLWCAPLSAQ IVPPPPADAE PLSAIDPALQ PVNSTKALSA SEQSVVRVLV
VYRGYGGVPL DSVGMGSGFV VAPGYIVTNY HVIETPPEAT SAEIYIVPHK GTGAAYQQVT
LVKPWLEGDL ALLRAEGLKI PPLKLSLVPQ KNQRIVTMGY PGITDRLLKR GGTELLEPAD
AYVTQGSIAL FASTNPDGSR VDTLFHTAPI NPGNSGGPLM DECGQVVGVN TWSAVSTLSE
TGDMDVPAGQ YVATHVSALY TFLQSTGVAV QTTSEPCFAK SEDEIIKDDG LSRALAAYRD
AQAKRLEEQR KAEQMNALMD QLQLGVLVLL SLLVVVLIAL IIRRRHPPKP KTPHTEAELP
HAEAHPHKAK AEKVHHKHPF PWGWIALAVF VVLIAAAFVL RESPVVQKMS QKAEVAAAKV
GPVRLTCDVD LKASPKPLAG VGPTDFEFDA AHACVNGRTP YEVQSNSTLL RFTVSDSEPT
AARLELSRDG LTFKRSDYRL TPEQHRDYVA QRAALGSLRC ASDKDTGQAE ALKDNMRKVR
QLAQSFLTFA PETETVWKCR KVPEPAAPKP
//
