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Database: UniProt
Entry: E7D102_9GAMM
LinkDB: E7D102_9GAMM
Original site: E7D102_9GAMM 
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
//
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