ID A0A101SJ92_9ACTN Unreviewed; 553 AA.
AC A0A101SJ92;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=AQJ64_44220 {ECO:0000313|EMBL:KUN75010.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN75010.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN75010.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN75010.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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:KUN75010.1}.
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DR EMBL; LMWW01000104; KUN75010.1; -; Genomic_DNA.
DR RefSeq; WP_059203552.1; NZ_KQ948800.1.
DR AlphaFoldDB; A0A101SJ92; -.
DR STRING; 1943.AQJ64_44220; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000052982; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 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 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, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 36..553
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023024189"
FT DOMAIN 83..124
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 224..374
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 378..552
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 368
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 553 AA; 57138 MW; C51F06114625EFEE CRC64;
MTSLYARHQR TTLAIATAVA AGALVTTGLT SGAVAAPTAS DAAAKPLAAP TALSASARTA
LIKDKQADAT ETAQEIGLGT KEKLVVRDVV KDADGTVHTR YERTYAGLPV LGGDLVVHES
AAGVNKGVTK ATKTTIKVAS LKAVVTAAKA EKQAVALAKD AGSAKTTADS APRKVIWAGN
GSKPVLAYET VVGGLQDDGT PNELHVITDA ATGKKLYEYQ GIETGTGKSL YSGTVSLNTT
LSGSTYQLTD GTRGSHKTYN KAHGTSSSAG TLFTDADDTW GTGAASSSTT DQTAAVDAAY
GAQVTWDFYK NTFGRSGIKN NGVAAYSRVH YGNAYVNAFW DDSCFCMTYG DGEGNVNPLT
SLDVAGHEMS HGVTANTAGL NYSGESGGLN EATSDIFGTG VEFYAANSND PGDYLIGEKI
DINGDGTPLR YMDKPSKDGG SSDYWSSSVG SKDVHYSSGV ANHFFYLLSE GSGSKTINGV
TYNSPTYNSS TITGIGRAKA LQIWYKALTT YMTSTTNYKG ARTATLSAAS ALYGSSSTEY
AAVAAAWTAV NVS
//
