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}.
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; 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
//