ID A0A1H4YEV2_9PSEU Unreviewed; 758 AA.
AC A0A1H4YEV2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Zn-dependent metalloprotease {ECO:0000313|EMBL:SED16387.1};
GN ORFNames=SAMN04489727_6693 {ECO:0000313|EMBL:SED16387.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SED16387.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SED16387.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SED16387.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNSO01000004; SED16387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4YEV2; -.
DR STRING; 208445.SAMN04489727_6693; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000199622; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR013783; Ig-like_fold.
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; PF05345; He_PIG; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:SED16387.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SED16387.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..758
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011490900"
FT DOMAIN 75..107
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 199..334
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 347..506
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
SQ SEQUENCE 758 AA; 77549 MW; 9A726661D2F10EA9 CRC64;
MHLRRPFVLA ASGALIAAVC TTTTAQAQPT TPNAVPDAQT LAVSAAAGLV ASRPAALHAS
ADDVFLAQKA ISATNGLKYI PYERSYKGLA VVGGDFVVAT DSTGQVLGTS VAQDQTINLA
TTTAKVSKDA AETTARQQLS AVESISPAQQ VVYALGTPTL AWKTTVVGRD AEGPSRLDVI
VDAATGKVLR TQEHVMNGDG TSAYNRPNPV HLDTTVSGST YSLKDPNLTN VSCQDAANNT
TFSGPDDLWG NGNATSRETG CVDALFAAQT EKKMLTQWLG RNGFDGSGGG WPIRVGLNDQ
NAYYDGSQVQ IGKNTAGQWI SSLDVVAHEL GHGIDDHTPG GISGAGTQEF VADVFGASTE
WFANEPSGGD VPDFLVGETI NLVGSGPIRN MYNPSALGDK NCYDSSVPNG EVHAAAGPGN
HWFYLLAEGT NPTNGQPTST TCNSSTITGL GVQSALKIFY NAMLLKTSSS SYLKYRTWTL
TAAKNLFPGS CTEFNTVKAA WDAISVPAQS ADPTCSATGT VTVSNPGNQS TVTGASVNLP
LSASGGTAPY TWSATGLPAG LSISSSTGTI SGTATTAGTS NVTVTATDSA GKPGTASFSW
TVGTTGGCSG QKIANGGFES GATSWTGTTG SIGQWGSQGQ AAHGGTYSSW LDGYGTTHTE
SIAQSVSIPA GCHASLTFYL HIDTAETTTS TAYDKLTVTN GSATLGSYSN LNKASGYVLK
TIDVSSAAGG TLALKFTGTE DSSLQTSFVI DDVAVTLS
//
