ID A1E8H1_MYXXA Unreviewed; 280 AA.
AC A1E8H1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 08-NOV-2023, entry version 55.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
DE Flags: Fragment;
GN Name=fibA {ECO:0000313|EMBL:ABL62796.1};
OS Myxococcus xanthus.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34 {ECO:0000313|EMBL:ABL62796.1};
RN [1] {ECO:0000313|EMBL:ABL62796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Weinheim1 {ECO:0000313|EMBL:ABL62796.1};
RX PubMed=18328701; DOI=10.1016/j.cub.2008.02.050;
RA Vos M., Velicer G.J.;
RT "Isolation by distance in the spore-forming soil bacterium Myxococcus
RT xanthus.";
RL Curr. Biol. 18:386-391(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF112165; ABL62796.1; -; Genomic_DNA.
DR AlphaFoldDB; A1E8H1; -.
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 Gene3D; 3.10.170.10; -; 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 Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 1..33
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 161..235
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 238..280
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL62796.1"
FT NON_TER 280
FT /evidence="ECO:0000313|EMBL:ABL62796.1"
SQ SEQUENCE 280 AA; 30819 MW; 0DB0D7726D8CBDC5 CRC64;
HYRYSVKHND IPVLGGELIL HARNGKVFAA NTNVRSDLRA ELKATIAGEI ATSAVDSDRE
TLKGWVTDKN PELVYWRVDD ELRLMYKVVQ HGNKADGTPV RDWVLVDARN ADVMLRIPQI
KESLDRRLHN GNNTSILPGA VVRIEGAVPV ADPVVNTNYD HLGTVYDCYN TLFGRDSIDN
VGGTLISTVH HRVNYVNAFW DGTQMVYGDG DGVTATNLAN SLDVTAHELT HAVTDNESDL
IYSGESGGLN ESMSDVFGAV CEWYGDGADE VSPRHWLIGD
//
