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Database: UniProt
Entry: A0A0Q8PKP6_9ACTN
LinkDB: A0A0Q8PKP6_9ACTN
Original site: A0A0Q8PKP6_9ACTN 
ID   A0A0Q8PKP6_9ACTN        Unreviewed;      1017 AA.
AC   A0A0Q8PKP6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Zn-dependent metalloprotease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE01_19025 {ECO:0000313|EMBL:KRB74083.1};
OS   Nocardioides sp. Root190.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB74083.1, ECO:0000313|Proteomes:UP000050886};
RN   [1] {ECO:0000313|EMBL:KRB74083.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB74083.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB74083.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB74083.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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:KRB74083.1}.
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DR   EMBL; LMIA01000012; KRB74083.1; -; Genomic_DNA.
DR   RefSeq; WP_056756604.1; NZ_LMIA01000012.1.
DR   AlphaFoldDB; A0A0Q8PKP6; -.
DR   STRING; 1736488.ASE01_19025; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000050886; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 2.60.40.2700; -; 3.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1017
FT                   /note="Zn-dependent metalloprotease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039343002"
FT   DOMAIN          111..147
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          271..361
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          364..518
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          20..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        445
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   1017 AA;  106574 MW;  4B53BCD2EB9AD3D9 CRC64;
     MRRVLALACA SALSVSLLAQ SPSGSAAPDP DDGERLLRSD ADGPLRIERS GADTTFVGTP
     VGTDVDNPTV SRGTSVSAAA RAHLTRYGGA VEADRSGTGL VETGSSEGAG GGDVVRYRQE
     IAGVPVLGAE VVVSVGADRE LTSLNANLSR SAGVRPAAVT ESMARDVAEG VLRRSGISDV
     RAADQGRWIL DPAAVGLDPA IGVRGVWRFE VRSGDHVRRL VLVDDRSGDV VLDIDLIQGI
     DRIVCDQANV RTNVVACSSA AAVRTEAPGG SSTADVEAAF QNAGAVSDFY REVIGLDLTT
     AIGLPSAQGR KLASTVRVCV TGPDSCPYDN AFWNGQAMFY GEGYAAADDV VGHEMTHGVI
     ERTSGLLYWD EAGAINESLA DIVGELVDHR NAGPGDSPTD WQLGEDLPGG ALRDMADPTL
     HHQPDRMTSP RWAADPSYED SGGVHTNSGV GNRAFQLISQ GGTFNGRTVT GIDAGDPTLL
     KSATLWLHTM AAITAFTEYA DLANVLDQTC TALIGHRGFT ASNCTAVRYA VAATEMALPP
     ATDPVKDAPR TCPAGSHPRT LLDSESGADQ ASLFGPAAGW GRTPETVVNS AYGVSAYSGD
     TAWVAADPAT PVTRALLSAA PVVVPEGQST YLAFRHWHLF DFSIDPSNGV GYWWDGGTAE
     MTAVDGTVYP LWDHPWDFGP TRTLQAPNAG RRAFGGSSRG WVGSRVDITA FGGMSVRPTF
     TMRTDSSYGA PGWYLDDILV YTCDRTLAVD VAPVLPDAAP HVGLPLTVSE PTWNLPGATT
     SHQWRRNGVP LAGMTQATYT PVPADVGTRL SVVVTGKLDD QVVPLVVTAS ADVETDAVPL
     TIVSAPTLPA TAPRVGKVYA VTAPIWNDPG TITTYQWRRD GVAIAGRTLR TYTPVAADAG
     RRLSVVVTGI LADQSVQLTA TSGIVARGLL VAPKTAGLSG TPRVGRRLAA VRGTWAPSPI
     TYSYRWFRGS KAITGATGSS YLLRKGDKGF RISVRITGSK SGYTAVTRTS GSVLVRR
//
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