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Database: UniProt
Entry: G5CEL1_9GAMM
LinkDB: G5CEL1_9GAMM
Original site: G5CEL1_9GAMM 
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
//
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