ID A0A1I6VKZ4_9BACI Unreviewed; 586 AA.
AC A0A1I6VKZ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Zn-dependent metalloprotease {ECO:0000313|EMBL:SFT14370.1};
GN ORFNames=SAMN04488145_113103 {ECO:0000313|EMBL:SFT14370.1};
OS Bacillus sp. 103mf.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761751 {ECO:0000313|EMBL:SFT14370.1, ECO:0000313|Proteomes:UP000198993};
RN [1] {ECO:0000313|EMBL:SFT14370.1, ECO:0000313|Proteomes:UP000198993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103MF {ECO:0000313|EMBL:SFT14370.1,
RC ECO:0000313|Proteomes:UP000198993};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FPAF01000013; SFT14370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6VKZ4; -.
DR STRING; 1761751.SAMN04488145_113103; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000198993; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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; 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:SF3; NEUTRAL PROTEASE B; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:SFT14370.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFT14370.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..586
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011584651"
FT DOMAIN 85..132
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 255..404
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 418..569
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 70..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65074 MW; D603FB2DECDF9078 CRC64;
MNYKKMTSAL LTFGLLCPLS TEAIHAQEIN NNQVKVEVAQ PGLTIGKLTE PQNDTKENIA
KKYLKGEVQG SKAQQEQVTT EKSVDFQPTN KETKENQTEV RLTQTYKSYK VYGQDLIVKV
DKNGVITTVS GKVAQNLAQQ PNLTITNFLS KNEVKTFLRN ALQTPNDALE KEFTSETVIY
KKQDGSYTYA DVITFTYENN DQIINGQAII DLIHSEMLFQ EKIVKNKEKQ PVPQAGIPQL
SSVKKHGAGV NALLEKILFN IAKGTDGKFY LADLTRGNGI YIYDANYADS QGGYDQAGYP
GTLVSSTSTT FADKEAVGVM KNMSAIYDYY KTKHNLKSYD NKDAKIVASV HGFDSTEVSD
GVKTNYENAF WHPGWNQMVF GDGLNGKLTS AIDVTAHEFG HAVFSGTTKN KVVKYPNDET
NALNEGLADF WGTQIEFYVK KDKGNWIMGD TLDGPTIRDI PNEIGDHGKK LYTNLQDFYN
DGNNQESHQN SGIISHVLYQ LVEGKTYNGV TVAKQSNDKV SKIVMRALQN YATSAEDFES
LHSHIVQAAK DLYGNAVATE VDKAFLAHGY KALPQVNEVI DVQNKK
//
