ID A0A0G3USH8_9ACTN Unreviewed; 1165 AA.
AC A0A0G3USH8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:AKL68763.1};
GN ORFNames=M444_28765 {ECO:0000313|EMBL:AKL68763.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL68763.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL68763.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL68763.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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DR EMBL; CP011664; AKL68763.1; -; Genomic_DNA.
DR RefSeq; WP_037792952.1; NZ_DS570407.1.
DR AlphaFoldDB; A0A0G3USH8; -.
DR KEGG; strm:M444_28765; -.
DR PATRIC; fig|465541.12.peg.6074; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
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; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR007484; Peptidase_M28.
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; PF04389; Peptidase_M28; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1165
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002560655"
FT DOMAIN 79..110
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 198..333
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 343..508
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 695..900
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 589..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 119454 MW; B815C72AED3EDFF3 CRC64;
MASVAAMALT ASLAGALAGT ASAAQPARER SQPAPTSAER AVAAADAAVR SGLDTLVNSP
RQQYERRLVT PWVQDLYSVA YERSYRGLPV VGGDAVVLAD GEGKVRAVQS ASARVIDVAT
TPTVTAKAAE ATSRSELAKV DKVLDSRLVV RLKDDKQVLA WETVLSGRTK TAPSKLHVFV
DARTGKVVDR HDEVVAGSGT SKWNGPNPLT IDTTAASGTY SLRDPNRPGL SCADYSTGSV
FSKSSDSWGT GNATSKETGC TDLMFAAQKQ WNMLSQWLGR NGVDGNGRSF PGKVGLSDLN
AYWDGSSVTI GRNSANEWIA GIDVVGHEYG HAIDSNTPGG TSGQESGLGE GTGDIFGALT
EAYANEPAPY DVPDYTVGEM INLQGRGPIR NMYNPPAVNN DPACYSSAIP GTEVHAAAGP
LNHWFYLLAE GTSPGGGKPS SPTCNSSTLT GVGVQSAGKI FYGGMLLKTS GMSYKKYRTA
TLSSAKSLDP TTCNLFNKTK AAWDAISVPA QSGDPTCTPS GQNDDFSMAL NPASGTVQQG
ASVTTTVATS TTTGSAQQVT LTATGLPAGV SASFSPATVQ SGQSSTLTLS ASSSAAPGPS
TVTVKGQGPS LAHTVDYALS VGGTTTPTDP PDVSVANVQA HLTQLNTIAS QNGGNRRAGS
AGYTQSLAYV KGKLQAAGYT VTEQNCTSCT YPSNNLIADW PGGPADQVVM FGAHLDSVSA
GPGINDNGSG SATLLENALV LAQKNPTLTK HVRFAWWTDE EQGLNGSKFY VGRLSSAEKS
AIKGYYNFDM VGSTNGGYFI NNVNSATAAP LKAYWTSLNL APEENTEGQG RSDDYSFQQG
GIPTSGYAAG ASARKTSAQA AKWGGTANAA YDACYHSSCD TTANISATVL DRSADGVAYA
IWKQAVGGDT PAQDFSISAS PAAGSAGPGG SVTSTVNTAT VSGAAQTVAL SVSGAPAGVT
ATLSPSSVQS GSSSTLTVQV GAGAAQGTYT LTVTGSGTTS HTTTYTLTVG GGGGTCTPRQ
LVVNGGFENG SAPWTATAGV ITNQSGEAPH AGSYMAWLNG WGSSRTDSAS QSLAVPSGCS
SYQLAFYLHI DTDEDENVVY DRFTVSVGGQ TLETLSNVDA GSGYALKTYD VSRFAGQTVT
LQFKGVEDQS LQTSFVVDDV TLQVS
//
