ID A0A0A7EI79_9GAMM Unreviewed; 934 AA.
AC A0A0A7EI79;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=OM33_13060 {ECO:0000313|EMBL:AIY66390.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY66390.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY66390.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY66390.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009888; AIY66390.1; -; Genomic_DNA.
DR RefSeq; WP_038643375.1; NZ_CP009888.1.
DR AlphaFoldDB; A0A0A7EI79; -.
DR STRING; 1348114.OM33_13060; -.
DR KEGG; pseo:OM33_13060; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_011878_0_0_6; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000030341; Chromosome 1.
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 CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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; PF18911; PKD_4; 1.
DR Pfam; PF04151; PPC; 2.
DR PRINTS; PR00931; MICOLLPTASE.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..934
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002027997"
FT DOMAIN 622..704
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 692..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 934 AA; 101475 MW; 210F5600FA160A6E CRC64;
MKLTKLALVI ATLSYGTSAL ANSAPTSENQ PKVHHHGVEF DRQDNAPTAV TSQHANLPFD
HAKNDLHTLH IEDMQQTFAA TSCNVNALAT SNSTQLINEI KSQGASCVNE LFGATSDIQK
AAYDSNNMYA VANHVKGLSQ SYQGGGDNDI EALFLYLRAG YYVEFYNDQV TFASWVKPAV
KGAIDAFVNN SHFYDDNDAH GKTLSEVLIT MDSSEQQDVY LPVVVEWLNR WNESYAAKWN
MRSAVNGVFT ILFRGQWNTE FKNKIGSAND LVSALAKFTT STYMIDSDAE YMIANAAREL
GRLKQYPGTI QTSVDAALNR IFSDYQMYGY GDSVWLGAAD TAGYHGSCDT YNICGFEQQL
ESQVLSQTYT CSSTIKIRSQ NMTSAQHQAA CSKMGYEETY FHGQLQTNNT PVADDVNSQL
QVNIFDSSND YSKYAGVIFG IDTNNGGMYL EGNPSTPGNI PNFVAYEASY ANPDHFVWNL
EHEYVHYLDG RFDLYGGFNA PTEAIVWWSE GVAEYIANEN DNQAAIDTIK DGSTYSLGTV
FETTYAGFDQ DRIYRWGYLA VRFMFERHRD ELNLMLASTR SGDWAGYKAR INTWAANYAN
EFTQWTQELA SGGDTNPPAN TAPVAVINGP YSGEVGTLIA FSSNGSNDKE SNIASYSWNF
GDGTTSSEAN PTHSYTTAGE YAVTLTVTDP EGLSSSEATT ATVTGSEPPV GNELQNGVAQ
QVTGNTGDEK RFVVNVPANA SDLEITLNGG SGDGDLYVKF GDAPTLTSYD CRPYVGGNSE
RCTIEQPQAG TYHVMVYGYA NFDTQVKANY TVQTGGGFNV PNACATEGPS GGGRLYDGDV
MCLAEQEPIW LSIADVSGAT SVAITTSNGS GDINLEYRNG GWPSAGNVDA SSQNVGNGEC
IYITNQSEYW GYVKVSGTAN GASIVVDFNT PGCR
//
