ID   A0A0H4C3Y4_9ACTN        Unreviewed;       939 AA.
AC   A0A0H4C3Y4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Metalloprotease {ECO:0000313|EMBL:AKN71555.1};
GN   ORFNames=QR97_18655 {ECO:0000313|EMBL:AKN71555.1};
OS   Streptomyces sp. PBH53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN71555.1, ECO:0000313|Proteomes:UP000036399};
RN   [1] {ECO:0000313|EMBL:AKN71555.1, ECO:0000313|Proteomes:UP000036399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBH53 {ECO:0000313|EMBL:AKN71555.1,
RC   ECO:0000313|Proteomes:UP000036399};
RX   PubMed=26227608;
RA   Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT   "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT   Urban Environment.";
RL   Genome Announc. 3:e00859-e00815(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA   Gosse J.T., Boddy C.N., Hill P.B.;
RT   "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT   urban environment.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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DR   EMBL; CP011799; AKN71555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4C3Y4; -.
DR   STRING; 1577075.QR97_18655; -.
DR   PATRIC; fig|1577075.3.peg.3841; -.
DR   Proteomes; UP000036399; Chromosome.
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; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:AKN71555.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AKN71555.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036399};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..939
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005205783"
FT   DOMAIN          110..138
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          279..441
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          444..598
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          267..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        525
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   939 AA;  98866 MW;  171C749A6B659697 CRC64;
     MRHSRTRSEH PVAAPRTRRH ALSGAAALLG AAALVVTAAP AGAAPAAPGT TAVGEGTATP
     ALVDGIREQA PVARTAADAA RAHLAAREDR YRIADPVRDL KPAGTLTSGG RQTVRLQQTH
     HGVPVLGGQY LVRMERAGGQ RIVTGTSGRY FTGLRTGTTA EIDDALAVER AVDAVRQDLT
     ARSFTAGPDG EDEGTPLAGT SHGLVVVPRG TGVLTRHITV RGTDPAHGEP VLREVYIDAR
     AGYPVLQYSG VRTFRAPGTA AARTRAARAR ADEPAPGTTG TGVRLDGTTV SLGITRDDAR
     DAYVLRDRTR IQSSPDRVLA TWDARGRWAS DLSGAWPEDL REFASPTERF GAEATDSGAV
     DAHWAAGQVY DYYRAKFGRD SLDGHGMTVN SLVGATDYGQ PYVNAFWDGR KMVYGSGDAE
     YRPLSAALDV VGHEMTHGVI EHSAGLVYAG QSGAMNEALA DYFGNAIESD ARHLSMDDPD
     SALLGETLCR TKDPRACAIR DLNDGRTTAG SFLGVGFGTD NGGVHLNSTI FAGALWDIRE
     ALGPDLADKI VYKALTEYLT PLDGFTQGRA AVVAAARQLK TGGQNLAAVQ RAFTAHGIVP
     NWEKALGIDS DVLLSRVNTY DTHLGAGGGW WVAANSNESG SEPYSVWAGR TDGKGQLKLM
     SPNDGRYHVN PATDGRTVVW QAHGPAGVDI LARPLAGGPV RTLWHGRSAG TALGVDGDVV
     AFAYSNHGGR AGVAHLSLKD PTHVETIGGG TYHRATFPSV HHGKIVYQDR RRVRAVYEST
     TRLIDVATGE ETVIQQAAPQ TSLGPTALTG DHVYWLLDAV GQNGTTTLRR AGLDGSGVTD
     LSPETGPDAR NVSEVTASAD AVTMVARTPA AETGNATLSK LWQFTPDRKG DGLRRSRVSC
     NRGEQLSAAA ADGTRVVWLD ATTGVSDVVT RARPSGTCA
//