ID A0A143H9L2_9BACL Unreviewed; 545 AA.
AC A0A143H9L2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=ATY39_00320 {ECO:0000313|EMBL:AMW97991.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW97991.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMW97991.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMW97991.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) 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|ARBA:ARBA00001947,
CC 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; CP014806; AMW97991.1; -; Genomic_DNA.
DR RefSeq; WP_066784105.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143H9L2; -.
DR STRING; 241244.ATY39_00320; -.
DR KEGG; rst:ATY39_00320; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000076021; Chromosome.
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; 3.10.450.40; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000076021};
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..27
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 28..545
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5022992139"
FT DOMAIN 92..141
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 249..394
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 397..544
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 545 AA; 59237 MW; CCF38D4A12C1A837 CRC64;
MKKGTSIALA LSLTVGAVLP FSSTAHATNS QNVLAAKIKE SGNEKNVTKK KGQAVPTFIH
GKLSNKPHKD KEAVKQFLKD NKETYPFDVE KDLTLLDVTK DEIGSKHFDF VQSVQGIPVD
GSALKVHTDE KGYVTAVNGD VFVEAGDYFK GKGKLKTNLS KKEAINNAWK SIDLTKDETL
VDFEVGPKGE KQSGTNEEGK QVIYKKGDNF YNAYKVNLQF INPYPANWVV YVDAETGSVI
DSYNAVTEGT GVGVLGDTKK LNTYYSSGTY YLYDTTKAMT GVIETRTAKN LSSLPGSYSV
DPDDNFNATN QRADVDAHYY AGVVYDYYKN TFNRNSFDNK GATITSTVHY GRNYNNAFWN
GSQMVYGDGD GTTFTSLSGS LDVVGHEITH AVTERTAGLE YQGQSGALNE SISDTFAMFM
DQKNFLIGED VYTPKIAGDA LRSLSNPTQY GQPENMSGYV NTTSDNGGVH TNSGIPNKAA
YNTIQSIGYD AAQKIYYRAL TVYLSPKSNF SAARAAMLAS AADLYGTGST QYNGVASAWT
KVGVN
//
