ID C9Z6V3_STRSW Unreviewed; 693 AA.
AC C9Z6V3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN OrderedLocusNames=SCAB_27921 {ECO:0000313|EMBL:CBG69893.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69893.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG69893.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69893.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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}.
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DR EMBL; FN554889; CBG69893.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Z6V3; -.
DR STRING; 680198.SCAB_27921; -.
DR MEROPS; M04.017; -.
DR KEGG; scb:SCAB_27921; -.
DR eggNOG; COG3227; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_008590_5_1_11; -.
DR Proteomes; UP000001444; Chromosome.
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:0004252; F:serine-type endopeptidase 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; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51829; P_HOMO_B; 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 Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 569..693
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 693 AA; 72041 MW; 4F89CC71DEEC5B2F CRC64;
MQKESVLRRQ SHRRTSHTGN TFGHSARRRA AAGALVAVTA LLAAAVQSGA ASAAPEKAPS
ASGKANPGAV SMKLTPAQRA ELIREANATK AETAGKLDLG SKEKLVVRDV VKDRDGTVHT
RYERTYDGLP ILGGDLVVKT SKAGATKSVV RATKAKIAVP SLTPTVTKAR AEKQALGAAK
AEKAKSPKVN SARKVVWAAS GKPVLAYETV VGGFQHDGTP QELHVVTDAT SGAKLYEWEA
VETGTGNTVY SGSVDLTTTQ SGSTFNLTDG ARGGHKTYNL NRGTSGTGTL FSGPDDVWGN
GSASNLESAG ADAHYGAALT WDYYKNVHGR NGIRGNGVGA YSRVHYGNNY VNAFWQDACF
CMTYGDGSGN ANPLTSIDVA AHEMTHGLTS NTAGLNYSGE SGGLNEATSD IFGSTVEFYA
ANSSDVGDYL IGEEININGN GTPLRYMDKP SKDGSSKDAW YSGIGNIDVH YSSGPANHFF
YLLSEGSGTK TINGVNYDSP TSDGLPVTGI GRAKAEQIWF KALTTKFTST TNYAAARTGT
LAVAGELYGT TSAEYTAVQN AWAGINVGSR PGGGGGGGTS FENAADVSIP DNGAAVTSPI
TVSGRTGNAP SNLAVAVDIV HTYIGDLQVQ LVAPDGTAYT LKAYGTGGSA DNINTTYTVN
ASSEVANGVW QLRVQDNAAR DTGYINSWKL TFP
//
