ID A0A1Z4RCB2_9CYAN Unreviewed; 363 AA.
AC A0A1Z4RCB2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=NIES4101_60610 {ECO:0000313|EMBL:BAZ40100.1};
OS Calothrix sp. NIES-4101.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ40100.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ40100.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ40100.1,
RC ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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}.
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DR EMBL; AP018280; BAZ40100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RCB2; -.
DR Proteomes; UP000290974; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 81..189
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 192..360
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 283
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 363 AA; 39975 MW; 1CEDB3E355FF5FBF CRC64;
MIRNHKKSLG FGWLGSQHNP SRCSVCCVIP PYMLEKVAIN GTETQRDWAF HALNLSSEFR
GRRKAVGSVN FAVSPGEKRR TIYDAGTSQS LPGKLVRGEG DPPSSDEAVN EAYDSAGATF
DFFSEIFDRN SIDNQGLRLD STVHYGLKYD NAFWNGDQMV YGDGDGELFQ RFTKCIDVIA
HELTHGITQY EAGLIYSGES GALNESMSDV FGALVKQWVK KQTAEQADWL IGEGLFTEKV
KGVGIRSMKE PGTAYDDPVL GKDIQPAHYQ DIYVGFKDNG GVHINSGIAN RAFYLAAMEI
GGYAWEKAGK IWYMALCDRL RSGSNFQRAA SIIVKVAGEL YGEGSNEQKA VQNAWEQVGV
SVN
//
