ID A0A517SSE8_9BACT Unreviewed; 939 AA.
AC A0A517SSE8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Protease 3 {ECO:0000313|EMBL:QDT59054.1};
DE EC=3.4.24.55 {ECO:0000313|EMBL:QDT59054.1};
DE Flags: Precursor;
GN Name=ptrA_1 {ECO:0000313|EMBL:QDT59054.1};
GN ORFNames=SV7mr_15600 {ECO:0000313|EMBL:QDT59054.1};
OS Planctomycetes bacterium SV_7m_r.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=2528025 {ECO:0000313|EMBL:QDT59054.1, ECO:0000313|Proteomes:UP000315003};
RN [1] {ECO:0000313|EMBL:QDT59054.1, ECO:0000313|Proteomes:UP000315003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SV_7m_r {ECO:0000313|EMBL:QDT59054.1,
RC ECO:0000313|Proteomes:UP000315003};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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; CP036272; QDT59054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A517SSE8; -.
DR Proteomes; UP000315003; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:QDT59054.1};
KW Protease {ECO:0000313|EMBL:QDT59054.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000315003};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..939
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021953060"
FT DOMAIN 78..224
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 236..409
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 537..661
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 689..869
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 25..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 105155 MW; 706E9CF463D5469F CRC64;
MNRCIRLVAL ASILIFQVSI SGSTREAQGQ DNRQPPQATT SQQQQEAVAK PGQQAPEGIM
KITEVEGISE YALENGTRVL LFPDPSKEVV TVNMTVFVGS RHEGYGEAGM AHLLEHMLFK
GTPEHPKIPK VLQERGATFN GTTWVDRTNY YETLPASEDN LKFALNLEAD RLINSFIRGE
DLESEMTVVR NEFERSENSP FRVLMQRMQS IAYDWHNYGQ STIGNRSDIE RVPVVSLRRF
YKKYYRPDNV MVIIAGKFDS ETALQLVSES FGKLESPETP IDPTYTVEPP KDGERTVALR
RVGDVQYVGT TYHVPAGGHP EFAAIKALSS ILGNEPSGRL YRDMVSTKLA SSVSSFAFAY
AEPGNLMCFA EIPNGNSIES ARAKLIEVQE QSFLTTPVTE AEVERAKQNI LKQRELQANK
TDQLAIQLSE WSAQGDWRLY FLYRDWVEAL TAEQVQAVAI KYLVRNNRTV GLFLPADQAE
RVQIPETPNL QAMLKDYKGR QVVQSGEVFD PDPIKIEART KRGELPSGLR FAMLPKQSRG
QSVSLSMTLR FGDQKSMINR LGAVELLGIL MARGTEDKSY EQLKDELTRL RATMQVSTFP
GVLQVSLETK KEYLAEVLEL LGEVLRTPAF KSEELEILRE QIITQIQQST TEPTALAPRN
VRRRLSPYGS DDVRYVQTLD EEIAMYRSAT REQIVALHDE LLSGQVGELS VVGDFDQQAV
MDAINASLEG WTTDTPYVRI DRPANGLEAG KLESVQTPDK ENAFFFASQE MSLSDSSPEF
APLELANFIL GGGGLSSRLA NRVRQQEGLS YTVRSSLSNR AKDKRVDWTV YAITNPDNKD
KLISVIQEEM DKFRDKGIEQ TELEQAQSAY LQAKRVGRTS DAALASELLQ GLFLGRTMKF
AAEHEQRIAE TTVDQVNAAI KKHLHWNKSA KAIAGDFSK
//
