ID E7D102_9GAMM Unreviewed; 403 AA.
AC E7D102;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Elastinolytic metalloprotease {ECO:0000313|EMBL:ADU33224.1};
OS Pseudoalteromonas sp. CF6-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=562716 {ECO:0000313|EMBL:ADU33224.1};
RN [1] {ECO:0000313|EMBL:ADU33224.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CF6-2 {ECO:0000313|EMBL:ADU33224.1};
RX PubMed=23012370; DOI=10.1074/jbc.M112.405076;
RA Zhao H.L., Chen X.L., Xie B.B., Zhou M.Y., Gao X., Zhang X.Y., Zhou B.C.,
RA Weiss A.S., Zhang Y.Z.;
RT "Elastolytic Mechanism of a Novel M23 Metalloprotease Pseudoalterin from
RT Deep-sea Pseudoalteromonas sp. CF6-2: CLEAVING NOT ONLY GLYCYL BONDS IN THE
RT HYDROPHOBIC REGIONS BUT ALSO PEPTIDE BONDS IN THE HYDROPHILIC REGIONS
RT INVOLVED IN CROSS-LINKING.";
RL J. Biol. Chem. 287:39710-39720(2012).
RN [2] {ECO:0007829|PDB:6IK4}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 231-403, AND DISULFIDE BONDS.
RX PubMed=31941905; DOI=10.1038/s41467-019-14133-x;
RA Tang B.L., Yang J., Chen X.L., Wang P., Zhao H.L., Su H.N., Li C.Y., Yu Y.,
RA Zhong S., Wang L., Lidbury I., Ding H., Wang M., McMinn A., Zhang X.Y.,
RA Chen Y., Zhang Y.Z.;
RT "A predator-prey interaction between a marine Pseudoalteromonas sp. and
RT Gram-positive bacteria.";
RL Nat. Commun. 11:285-285(2020).
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DR EMBL; HQ005379; ADU33224.1; -; Genomic_DNA.
DR PDB; 6IK4; X-ray; 1.90 A; A=231-403.
DR PDBsum; 6IK4; -.
DR AlphaFoldDB; E7D102; -.
DR SMR; E7D102; -.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR000841; Pept_M23A_Blytic.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR PRINTS; PR00933; BLYTICPTASE.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6IK4};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR600841-3};
KW Hydrolase {ECO:0000313|EMBL:ADU33224.1};
KW Metal-binding {ECO:0007829|PDB:6IK4};
KW Metalloprotease {ECO:0000313|EMBL:ADU33224.1};
KW Protease {ECO:0000313|EMBL:ADU33224.1}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0007829|PDB:6IK4}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003216569"
FT DOMAIN 276..360
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:6IK4"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:6IK4"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007829|PDB:6IK4"
FT DISULFID 293..339
FT /evidence="ECO:0000256|PIRSR:PIRSR600841-3,
FT ECO:0007829|PDB:6IK4"
FT DISULFID 383..396
FT /evidence="ECO:0000256|PIRSR:PIRSR600841-3,
FT ECO:0007829|PDB:6IK4"
SQ SEQUENCE 403 AA; 45417 MW; 1FD9245A63745E90 CRC64;
MNKHLLTLAV TTGLGFSSIA FAGVHNHETF EFSDQAVEQL NLNSLLIMDD QTFVFNNDLL
NEDWDNYFAS YAPELQSKQA FILHWAGYYS INPKVILALI EQQSEGLSDP SVELESVFKN
ISDKQGFEEQ VKDVVFKLSQ RFYAFKHWQE QAVKHDKNSN SIKHLIRPSQ VSTAATAALA
SMMSKQHNLH GQANDSLTRF LDIFEQLSPE QSLILNTDQV TFSGEEQSVQ ATFTMNLPWS
QGYYWYSGGA HSNTGSGYPY SSLDFNNGSG GWGSNTPWVQ AAHGGVITRF SSCNIRVTHS
SGFATNYYHM SNLQYNNGDT VQPGTLLGRY ANSYNQALCE GGQSSGPHVH FTLLQNGQQV
SLHNRYISNY RIDVGNSNYD SNCNNFYFER NGRRTCAWRP LYR
//