ID V4PYG2_9CAUL Unreviewed; 595 AA.
AC V4PYG2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABENE_05905 {ECO:0000313|EMBL:ESQ93436.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ93436.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ93436.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ93436.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(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:ESQ93436.1}.
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DR EMBL; AWGB01000008; ESQ93436.1; -; Genomic_DNA.
DR RefSeq; WP_018080496.1; NZ_AWGB01000008.1.
DR AlphaFoldDB; V4PYG2; -.
DR STRING; 1121022.GCA_000376105_00829; -.
DR PATRIC; fig|1121022.4.peg.1175; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000017837; 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 Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..595
FT /note="Serine protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004727590"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 361..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 63356 MW; B7F82A6516F97C6B CRC64;
MVMAAASLLC LTTASLPSLG WAQSDSAESN PSIAQQIADS DLQPVNSTKA LRSSEQSVVR
VLVVYRGYGG VPLDTVGMGS GFVVAPGYIV TNYHVIQVPP EASSADIYIV PHKDSGASYQ
PVQLVKPWVE GDLALLAAPG LKIPPLKLYL TPYKNERVVS MGYPDVTDHL LNRSGTALLE
PADAYVTQGS IALFASTNPD GSRVETLFHT APINHGNSGG PLLNECGQVV GVNTWTAPST
MSAGGNLDIS AGQFVATHVS ALNTFLSSAG VSPGLVSAPC YAKSEDEIVK DDALSRVLAA
AAEAQVQRLA EQKKAEADRA TLERLQLGAM IVLSGLVLVL IGLIIRREIL HRAEIHRKEH
GAPTAFSDEA PSESPKPGKT KPVRAERVRT DHLEKVRTAI TSRVKHPIPW GWIFLAAVII
IAVATFLIKD HDIYRRLTKP KVAAPVAAAA AVHMVCAIDK AASSNPLSDA GPVEFDFDAI
HACVNDRTPY EPQANGTLLR FTTGDANPVA ARMELAADAT TFIRYEYRME PAQYAAFKGQ
MSALGSFRCS AHADQGALTA LADNLARVRG LSQTYLTMAP ETKTVWRCAP QTGQG
//
