ID A0A136JWY4_9BACT Unreviewed; 355 AA.
AC A0A136JWY4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=prtS {ECO:0000313|EMBL:KXK01671.1};
GN ORFNames=UZ03_NOB001002163 {ECO:0000313|EMBL:KXK01671.1};
OS Nitrospira sp. OLB3.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXK01671.1, ECO:0000313|Proteomes:UP000070691};
RN [1] {ECO:0000313|EMBL:KXK01671.1, ECO:0000313|Proteomes:UP000070691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB3 {ECO:0000313|EMBL:KXK01671.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-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:KXK01671.1}.
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DR EMBL; JZQY01000045; KXK01671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JWY4; -.
DR STRING; 1617410.UZ03_NOB001002163; -.
DR PATRIC; fig|1617410.3.peg.2202; -.
DR Proteomes; UP000070691; 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; 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; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 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|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}.
FT DOMAIN 76..184
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 189..354
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 355 AA; 39279 MW; 30D9F5AF9D0F5C69 CRC64;
MQIDQRTHSS ECQTFCSIIP PYVFDQLAKS DDSKVRQLAI DAIAAGSAAR AVRSTLAMMA
GWAAVPSPSA KCHRLVYDVK HGNFNDLPGT LMREERDPRS DDPAVNEAYT HSGTTYNFYK
KVFQRNSLDD RGMSLISSVH LGRNLNNAFW TGEQMCYGDG DGRIFIRFTK SLDVVGHELS
HGIISHTCNL VYSNEPGALN EHFADVFGSL VKQWRRRQSV KSADWLIGND IMGPATTAKS
LRTFKAEKAY ENDPLLGTDP QPKHLRNKYN GSSDNGGVHI NSGIPNHAFY LVATEIGGKA
WERAGQIWYK TLLKLTSTSQ FHDMVESSTE TASTLYGAGS AEYKAVVKAW KAVGF
//
