ID E6S9D2_INTC7 Unreviewed; 1136 AA.
AC E6S9D2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:ADU47108.1};
GN OrderedLocusNames=Intca_0563 {ECO:0000313|EMBL:ADU47108.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47108.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU47108.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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DR EMBL; CP002343; ADU47108.1; -; Genomic_DNA.
DR RefSeq; WP_013491429.1; NC_014830.1.
DR AlphaFoldDB; E6S9D2; -.
DR STRING; 710696.Intca_0563; -.
DR MEROPS; M28.003; -.
DR KEGG; ica:Intca_0563; -.
DR eggNOG; COG2234; Bacteria.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_289316_0_0_11; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000008914; 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; 2.60.120.380; -; 1.
DR Gene3D; 3.10.170.10; -; 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; 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; PF04389; Peptidase_M28; 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.
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:UP000008914};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1136
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039438271"
FT DOMAIN 95..128
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 220..356
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 366..530
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 715..921
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT ACT_SITE 349
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 1136 AA; 114757 MW; C34A5A41EADE644C CRC64;
MTRPLPRRLG RLVALGSLAG LATPLALQAP LAAAVPPPLA GNAPPATVGS ALAGQPSKDK
ALAAADAAIQ RSLGAVAASG GEAFIRQTAN PGPGGRYYVL YQRSWKGLPV IGADAIVTAD
ETGAVRDITH ATDRVPSVAS TRPSVSAGSA AAAATALVAT VDHVEGPDLV IFMGDGKAPR
LAWHVRVEGE RASGRPAVLE AYVDARSGKV ISAEDLVREA TGYGHHNGTV SITTTGSGSS
YSMASTSAPG LKCQNQSGTT YTDSDNVWGN GSGTDLPTAC VDAVYGGEQE ELMLAAWAGR
NGINGSGSNY PARVGLADVN AYWNGSYANF GHNQAGTKQA TPMDVVAHEF GHGVFQFSGG
SGGSGNEAGG LNESTGDILG AATEFYAGNA SDPGDYLVGE EVDLVGQGPI RNMYDPAALG
DPSCYSADIV NTEVHAAAGP QNHWFYLLAE GNNPGGGKPS SPICTGGPSS VTGIGVQKAT
NIFVNAIQRK TSPWTHAKAR VATLQATKDL YPGSCTEFNT VKAAWLAVAV GPQSTEPTCT
ASSQDFAMTL SPTSGSIDAG ASATATVATT TTSGSAQSVT FSATGLPSGA TVAFSPQTIT
SGASSTMTIA TSTSTPAGTY TVTVLGDGAA IDRTATFTLA VGGGTPGPTA PDIDVEKVKA
HLSALQTIAT SNSGNRRAGS PGYTASVAYV KDKLTAAGFT VTLQRCTSCT YPSDNIIADW
PGGDPNRTYV FGAHLDSVSS GAGLNDNGSG SAAILETALA LARQNPTMAG HLRFAWWTDE
EQGLNGSDFY VRSLTSTQRS QIKAYYNFDM VASTNGGYFV NHVTSAAAAP MKAYWDGLGL
APEENTEGAG RSDDYSFEAY GIPTSGYAMG ASARKTSAQA QKWGGTAGAS YDPCYHSSCD
TYPSNVNATG LNRAADGIAH TAWAQAVGTD TQPGDDFSVS VSPTAGSVEA GSSTTATVRT
AVTSGSAVTV TLSVSGLPAG TTATFSPATV TAGGSSTLTI SSSSSTPAGT SNVTVTAVGG
GKSHTAGYAL TVTSTASGCG GYDVVQSGTV TSGGTTYLPY VYDSTAGVMT ACLDGPNGVD
FDLYLQKWNG SSWSTVASST TSAPDETLTY SNTAGYYRLA VKAYSGSGSF TTGISG
//
