ID A0A0Q5E7L8_9BURK Unreviewed; 621 AA.
AC A0A0Q5E7L8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=ASF61_01675 {ECO:0000313|EMBL:KQQ47385.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ47385.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ47385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47385.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ47385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47385.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQQ47385.1}.
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DR EMBL; LMNW01000001; KQQ47385.1; -; Genomic_DNA.
DR RefSeq; WP_056150495.1; NZ_LMNW01000001.1.
DR AlphaFoldDB; A0A0Q5E7L8; -.
DR STRING; 1736266.ASF61_01675; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
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 CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
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; PF07504; FTP; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 20..621
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023159700"
FT DOMAIN 83..119
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 267..430
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 434..613
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 19..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 424
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 621 AA; 65773 MW; 892DB71E24F9C774 CRC64;
MNRSTSLLLL SALAGTAMAQ PLPPSSASSS PLMGGPVAPP SPQQTATLLA RLAALDRAND
PRRTLAPQAD RQSYRIAAHH PGAAGQTIAR VQHTYQGLRV FGSEAVVVTD PAGAIVSASV
TDRRPGAQSL AAGGTAPPAP ADVTPKLTPQ QAIAAAIRPV RDRVETIEHR WQPVAELLLY
PVVTSAPTIA AAAKPDAELN ALDVQEVVQR YALAYYVRTR MVKGRQPRQL LYHDTIVDAR
TGEILAQWQA LQTADHSGTG TGTGTGTGTG NSQYNGVVAL STSQDGQQFR MLDTTRGKGG
RFGGMAITNA DHSAMHNPDP GQVYASASNS WGDGKQYTGG STTDANGQTA AVNAFWGLMN
TYDTNRNVLG WQSLDGNNTA THIAVHVDRD YDNAFYDDRC KCMFIGDGGS YFYNLGSIDV
IGHEMSHGVT AATADLVYAG ESGGLNESHS DIGGEMVEAY ARGGGAGATI PARGNDWLVG
QEISRDSKPL RYMIKPSLDG RSADAWSTGL KKLDVHYSSG PNNRMFYFLA KGSNADPASD
AYSKYLVKSP QAMTGIGNDK AYRIWFRALS TKFTSSTNYA AARARVLEAA QELYGAGSKE
AVAVQRAYAA INVGADIDEA R
//
