ID B1VXH8_STRGG Unreviewed; 752 AA.
AC B1VXH8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN OrderedLocusNames=SGR_1615 {ECO:0000313|EMBL:BAG18444.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18444.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG18444.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Digestion of native collagen in the triple helical region at
CC Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for
CC Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala
CC or Arg at P3'.; EC=3.4.24.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000424};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AP009493; BAG18444.1; -; Genomic_DNA.
DR AlphaFoldDB; B1VXH8; -.
DR KEGG; sgr:SGR_1615; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_011878_0_0_11; -.
DR Proteomes; UP000001685; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR PANTHER; PTHR13062:SF9; A2M DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13062; COLLAGENASE; 1.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF08453; Peptidase_M9_N; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00931; MICOLLPTASE.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 99..280
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 672..738
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 502
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 752 AA; 81417 MW; 5F438A36643D042E CRC64;
MGLALLAQPA QAQPNSPSAA TASNASQPSR PAGSADLAPQ AQQSPTSDPG HQAEGRSKAS
QLPPLSADKS PLKEAHGEHD APSEQGADGK SRAKAAAACD PADFTGRTGS ELVRFIRAST
TDCVNTLFSL TGSSARLAFR EAQMTSVAYA LRDNAAYYPG DGSTGTPQLV LYLRAGYYVQ
WYNPDVVGPY GPTLRTAIRS GLDAFFASPR SRDVTDDNGE TLSEAVILID SAQENARYIS
VVKRMLADYD STWNAFSRML AAVNNVYTVT FRGHQVPAFV SAVEADPSLI DALHRFAADH
LSLLEGDQSY LTSNAGRELG RFLQHAGLRS KVRPLATALL RDTSLTGPTA PLWVGIAEMA
DYYDKANCAA YGVCDLQERL KREVLPVRHT CSPSIRILAQ QMTSAELNAS CTSLIEQDAY
FHRIAKDSGP VADDNNTTIE VIAYDSSTDY QTYAGAMYGI DTNNGGMYLE GDPSAAGNQP
RFIAYEAEWL RPDFHIWNLN HEYTHYLDGR FTMYGDFAAN MTTPTIWWVE GFAEYISYHY
RQEPYTAAMT EAGKGTYALS TLFSTDYSHD TTRVYRWGYL AVRYMLEKHP ADMDKVLAHY
RAGQWSAART YLTTTVGTRY DSDWRTWLAG CAAGDCGGGD GAVTECADSD PRVLGQNCRR
SNLSATTGNY SYHYLYVPAG TKQLKITVSG GTGDADLYYS GSGWATTGSS TQRATGAGNS
HTLTISNPRS GANYISLHAV ASFGGATVTT AY
//
