ID A0A0C5UZW0_9GAMM Unreviewed; 1353 AA.
AC A0A0C5UZW0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Zinc metalloprotease (Elastase) {ECO:0000313|EMBL:AJQ92835.1};
DE EC=3.4.24.25 {ECO:0000313|EMBL:AJQ92835.1};
DE EC=3.4.24.26 {ECO:0000313|EMBL:AJQ92835.1};
GN ORFNames=YC6258_00785 {ECO:0000313|EMBL:AJQ92835.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ92835.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ92835.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ92835.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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DR EMBL; CP007142; AJQ92835.1; -; Genomic_DNA.
DR RefSeq; WP_044615805.1; NZ_CP007142.1.
DR STRING; 1445510.YC6258_00785; -.
DR MEROPS; M04.019; -.
DR KEGG; gsn:YC6258_00785; -.
DR PATRIC; fig|1445510.3.peg.769; -.
DR HOGENOM; CLU_252503_0_0_6; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000032266; Chromosome.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR CDD; cd00146; PKD; 3.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR045474; GEVED.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF20009; GEVED; 2.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF18911; PKD_4; 4.
DR PRINTS; PR00730; THERMOLYSIN.
DR SMART; SM00089; PKD; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49299; PKD domain; 5.
DR PROSITE; PS50093; PKD; 5.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AJQ92835.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:AJQ92835.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AJQ92835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1353
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002183423"
FT DOMAIN 605..658
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 821..875
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 899..951
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1006..1044
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1276..1314
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 1353 AA; 150511 MW; A839FAD879B17649 CRC64;
MFRNIRLLSG LLLGLGSVAA YSAEPVSVFD QLSSPSVSTF KRSSSQSVTA DDGSALAKML
HRQLNLDDDA QLVEQGHSQA GEQHSFSYQL QYLGLPVFDY TIAVITTSSG HVVQGYGQLV
RSLAADLGDV EVLTEEQMDL HAQAYIHQRY HDEPRFFDHK TVKQGVYIDP QGQAHDAIQL
IFFTDLLQGI SAPEKMRVYL NATTGSTLSE ANILMHYQAA GSGPGGNEKV EQADYAFVAG
DVSGQSVKDL RTFVVEKQND ACAMELSGKL KTFDAKHKTS NLPENVHRYD CGSDNAENRH
TEALTNTAKS ALNDAHYHGQ VTIEMFERYL GQKPYFHEAV KQYVHYGNNY DQAFYDEGQV
HYGDGEYLFY PLVALDVVAH EIAHGYTLGY GSGKPAKMML NGEARAINEA FSDMAGEAAE
YYLNGENDWR SNYDSYQGSG ALRYFEDPTA DGDSVGHVDD YYDALDSHYG SGIFNKAFYL
LATNGGEAQP VAGDWNTQYA FMAFATANQN CWVASSTFQQ AADCVVRWAP SVVQTAMQAD
GVKGPDGQVW SKNALKNQIR KAFASVGIQL DLENQQGVES RFEREIHFLT VSFSNQSRYE
NKVLAANDAT WQWDFGDGQV STTHSPTHTY AQTGHYNVRL TVTMNDGETD TVWLPVDVVE
HYCSVSGTDP EQYYASSVMF NNTEFVTNGD AEISYRDYSD QAVMVPVGQQ VFYALKMGQH
SNTADYAKRV QIWLDKNRDG QFSIASEQMY AGSAVDELSG VLAFTGEPGQ DYRVRIIVSF
ALFDRLPCDQ IRSASIQDYT LRWDDAASSY INIQVEHRTN KVHFSNLTED NRVTSWDWQF
GDGGSSHEKS PTHDYWRSGS YQVTAIAKAS DGSEVGRWDE TIAFTTVTQP VIKFDANDQT
VEFDASDSVM PEGTTIHWDF GDGTTDKDNK NKVSHDYVED GLYDVTLTLT NEDNPSGATS
QQQVSIGFNP NFYVQSIERQ DDGRYRVVFR NNTVDPGDNH GKWLLRWDFG DGQVSEESEY
DSLNQSIIHV YSKPSNNPYS VTLSIKYLSA DTSAWVSKSV TVELTIDNDS PDTGDPDGYC
EPIFDAESEW IKRIIINGQA FDSDAEGGLV NPDIPIRLVA GEQVSYRIES GYIEGGPYAE
NYHVWIDLNG DGQFGDGHWK TDKSERVLKV YDHTNDDQGN GYVEGYFQVP TIKKDKPFTT
RMRVLQLFGY SKIDTINPCS NYPASDANGE VEDYLVTISA SFDNSIPDLK LHVEGLTLSF
DTSASIYPEG AISKVTFGDG DSSTEDKGKH VYKKSGDYLV TLRIYDESDN EINAIGKTVT
AENKESASGS HGGIEWLVLL PLLLLKRKNL FKF
//
