ID A8H687_SHEPA Unreviewed; 972 AA.
AC A8H687;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN OrderedLocusNames=Spea_2754 {ECO:0000313|EMBL:ABV88074.1};
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88074.1, ECO:0000313|Proteomes:UP000002608};
RN [1] {ECO:0000313|EMBL:ABV88074.1, ECO:0000313|Proteomes:UP000002608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) 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; CP000851; ABV88074.1; -; Genomic_DNA.
DR RefSeq; WP_012155980.1; NC_009901.1.
DR AlphaFoldDB; A8H687; -.
DR STRING; 398579.Spea_2754; -.
DR KEGG; spl:Spea_2754; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_011878_0_0_6; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000002608; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; -; 2.
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 InterPro; IPR028974; TSP_type-3_rpt.
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.
DR SUPFAM; SSF103647; TSP type-3 repeat; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABV88074.1};
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:UP000002608};
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..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..972
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002720722"
FT DOMAIN 111..288
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 892..957
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 38..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 972 AA; 106567 MW; 3358EA496198C676 CRC64;
MSIKSSKSQA KKGQFKVHAL ALACSAILFP SAALATSEVA PTEKASSKAA HGKDLKSRFE
KGANVPGKQK NAEKTQRQNI DKSKEQKVEG PMGAVGSVGP AAESEAEVCS SELAALSGQE
LFNYVREADI SCISALYSRN DAVSVAAYQT ENVVSVANQA ASMAATYDSS TGYEMRNLFY
FLRGAFYIEF YNDDLTYSDT LAADAVYGAL VEYSKNPKLF EITHSAGDTL MEFFTSWSSA
DRILESVPLI TDYLQMFNAD FLASNRHRAA MTSALTTLYY GSWAEDYNKL AMEHGELIDA
LLNIATADYI INSDYQYEST DAFHEFGRFY EYQAYWDLPQ SLKTRLNDGV ELYMSKFERM
SAEWADGAGY LDYYNPGDCE QFGICGWEEE LEQTALPINY NCSDTIYIRA QQLTNDELQA
SCDLMGGEET LFHNVLATGY QPVADDLNES LEVNIFDSYD DYAQYAGVIF GISTDNGGMY
LEGTPSQEGN QARFIAHEAT WTEDILVWNL KHEYVHYLDG RFNQYGAFNY FDIDTGKSVW
WSEGLAEYIS KQNRNDGAVD MGRSQAYSLS EILANTYNSG SDRVYSWGYL AVRFLFENHR
SDVDELLVLA RGGDADGWLA YIDNTIGQNY NSEWNTWLTS VTSNDESIAI DITDPIDSDG
DGVADDQDAF PHDPSETRDT DGDGVGDNAD AFPTDASETV DTDGDGVGDN GDVFPTDPTE
WADSDGDGIG DNADTDEPNK PVEHCGVATI RDGKLTQDKV ECVEGTDINY FYTYVEEDNT
PLYISTSGGE GDVDLFFNQD IWAKPSDFDA RSENDGNEES LSVIANSGWV YVSLLAHQDF
DGVSLKVSLT EEGDTGTTPV AVADACATQS PYSYGGVEFG EAICIEDGHS SYYFYVPTGT
EEVTVASGHG SGNVNLYGNS QTWAGPDSFE VKSENADNVE SLTISAPAEG WYYISADGAP
SSEGASLVVN IK
//
