ID A0A1S1MVB5_9GAMM Unreviewed; 933 AA.
AC A0A1S1MVB5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=BET10_19025 {ECO:0000313|EMBL:OHU88908.1};
OS Pseudoalteromonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU88908.1, ECO:0000313|Proteomes:UP000179786};
RN [1] {ECO:0000313|EMBL:OHU88908.1, ECO:0000313|Proteomes:UP000179786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW1 {ECO:0000313|EMBL:OHU88908.1,
RC ECO:0000313|Proteomes:UP000179786};
RA Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT seawater.";
RL Submitted (SEP-2016) 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}.
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:OHU88908.1}.
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DR EMBL; MKJU01000030; OHU88908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1MVB5; -.
DR STRING; 1859457.BET10_19025; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000179786; Unassembled WGS sequence.
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 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..933
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010181958"
FT DOMAIN 625..707
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 25..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 933 AA; 102335 MW; 632660586AE4213C CRC64;
MMKLNKIALA LPVLGMSLNL TVSAAQHSGS APTQPQTEQS VQHIHHGHEH EQVDERAPVA
ASQLQDVTRI NPQLKLQQVM SSQASEAALS CDASAFANSS GSQLVEQVKS QGSNCVNELF
TASSSDQVAI FTSSKMNTIT DHARTLATSY TGLGGDELKA MFLFIRAGFY VEFYNDAVTF
DSQVAINVKS AIDVFVNNSH FYDNNDEHGK VLQEVITTMD SAELQHEYID VVRQWLLRFD
ENYANNRNMR NAVNGIFNIL FRGQWNSEYV TKIKTDSALV SALVAFTQKS WMVGSDSEFL
ITNSAGELAR LTQYRPSDID EAVTNGLKTL FSTYKSYGYG DSLWLNAADV ASYFGHCSEF
NICNFEENLT QQVLSQIHQC SSTIRIRAQE MTAVQLSSAC DTMAAEETRF HTRLATNQTP
VADDNNSFLQ VNIFNSSNDY KKYAKVIFNI DTNNGGMYLE GDPSKTDNQA NFVAYEASYA
KADHYVWNLE HEYVHYLDGR FDLYGGFNAP TEDIVWWTEG VAEYIANQND NQAAIDTIKD
GSVYNLQQVF ATTYDGFDQD RIYRWGYLAV RFMFERHNDE VNKMLGKTRV GDWTGYKSLL
NGWQVAYDAE FTQWTQELAG DVNTAPVAEV NGPYSGVAGE PVSFSSNGSS DAQGPIASYL
WDFGDGNQSQ QANPTHTYNA AGDYTVTLTV TDSEGLSNSA STSAQIEQGQ SVPQLQRGQA
VTINGAQDEQ LLFVLSVPQG ASDLNIAISG GDGDADLYVR YGSEPTLSSY DCRPYVGGNS
EQCDFATPQE GQYYVMIRGY NAFNNVSLVA NFDAPIASLP DACQTQAAKT GGRATAGELI
CLGDQSVMWF SLENVSGQDT VRIETANGSG DLKLEYSNAG WPDGSNVDAT SDNLGNAECI
SVSAQSQYWG YLKISGDSQA ASLKVTYNEG GCN
//
