ID A6FBW4_9GAMM Unreviewed; 622 AA.
AC A6FBW4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=PE36_17030 {ECO:0000313|EMBL:EDM67386.1};
OS Moritella sp. PE36.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM67386.1, ECO:0000313|Proteomes:UP000004278};
RN [1] {ECO:0000313|EMBL:EDM67386.1, ECO:0000313|Proteomes:UP000004278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE36 {ECO:0000313|EMBL:EDM67386.1,
RC ECO:0000313|Proteomes:UP000004278};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JUN-2007) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDM67386.1}.
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DR EMBL; ABCQ01000013; EDM67386.1; -; Genomic_DNA.
DR RefSeq; WP_006031876.1; NZ_ABCQ01000013.1.
DR AlphaFoldDB; A6FBW4; -.
DR STRING; 58051.PE36_17030; -.
DR MEROPS; M04.016; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000004278; Unassembled WGS sequence.
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; 2.60.120.380; -; 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; IPR025711; PepSY.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF04151; PPC; 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, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 25..622
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5022985016"
FT DOMAIN 62..111
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 167..202
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 220..358
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 361..505
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 546..608
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 351
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 433
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 622 AA; 67328 MW; E049622186B71DAD CRC64;
MMANNKFILS AVAVSLLGTV NAIAAERVNL RDNIQQLASA ALADPGILMS APAQLLGLSW
NDGLSVIKTY RNSKGDSITR YQQTYFGLPI IGEQAIIART SKGLFKRAHG AILNNIADDI
VDITPSITTV NALRQAKRLS RPATPLAENK SVATENETSR LAVWLGDDGV AKLVYEVSFF
QRADKPSRPY YIIDAHSGEV LLSYDNLQTA DATGPGGNEK IGEYRYGSDF SALNVTQAGG
ICVMNNAQVK TVNLNHGTEG SDAFSFTCPE NTVKSINGAY SPLNDAHYFG GIIFDMYKDW
LNVSPLTSQL VMRVHYDKNY ENAFWNGESM TFGDGADIFY PLVSLDVSAH EVSHGFTEQN
SGLVYSGKSG GLNESFSDMA GEAAEFYMHG RNDWLVGGQI LKANGALRSM SHPPMDGSSI
DNQADYRFNM DVHHSSGVYN KAFYTLATTA GWDTQKAFVL YAAANQYYWT SNSNWNDAGN
GVMDAACDLD YNVDDVQASL TAVGVVADVS DGSQCSVTKP PVSAIDRTEE NISTSFFRPA
NFKQELGEGY SRLIVTLAGG TGNADLYVKH EDKSLFSKSD CISKTPGNIE TCVIDNPNAG
IWKIDVRGYG STSGVILNIQ AQ
//
