ID G5CEL1_9GAMM Unreviewed; 175 AA.
AC G5CEL1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
DE Flags: Fragment;
GN Name=proA {ECO:0000313|EMBL:AEQ27926.1};
OS Legionella cincinnatiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=28085 {ECO:0000313|EMBL:AEQ27926.1};
RN [1] {ECO:0000313|EMBL:AEQ27926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43753 {ECO:0000313|EMBL:AEQ27926.1};
RX PubMed=21948093; DOI=10.1099/ijs.0.035709-0;
RA Edelstein P.H., Edelstein M.A., Shephard L.J., Ward K.W., Ratcliff R.M.;
RT "Legionella steelei sp. nov., isolated from human respiratory specimens in
RT California, USA, and South Australia.";
RL Int. J. Syst. Evol. Microbiol. 62:1766-1771(2012).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR EMBL; JN086180; AEQ27926.1; -; Genomic_DNA.
DR AlphaFoldDB; G5CEL1; -.
DR MEROPS; M04.006; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 2..67
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 70..166
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEQ27926.1"
FT NON_TER 175
FT /evidence="ECO:0000313|EMBL:AEQ27926.1"
SQ SEQUENCE 175 AA; 19543 MW; 4D0C9EE89C4B11D6 CRC64;
ADWYGVNVLS NSNGSPMQLV MRVHYGDGYE NAYWDGEQMT FGCGDRMMYP LVSLGVGAHE
ISHGFTEQHS GLEYYGQSGG MNESFSDMAA QAAEHYSVGK SSWQIGGEIM KESSGYDALR
YMDKPSRDGE SIDTADEYYG GLDVHYSSGV YNHLFYILAN QPNWNTRMAF DVMVK
//