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Database: UniProt
Entry: R4T0K6_9PSEU
LinkDB: R4T0K6_9PSEU
Original site: R4T0K6_9PSEU 
ID   R4T0K6_9PSEU            Unreviewed;       627 AA.
AC   R4T0K6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:AGM04537.1};
GN   ORFNames=AORI_1949 {ECO:0000313|EMBL:AGM04537.1};
OS   Amycolatopsis keratiniphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX   NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM04537.1, ECO:0000313|Proteomes:UP000013968};
RN   [1] {ECO:0000313|EMBL:AGM04537.1, ECO:0000313|Proteomes:UP000013968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM04537.1,
RC   ECO:0000313|Proteomes:UP000013968};
RX   PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA   Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA   Ding X., Zhang L., Zhao G., Zheng H.;
RT   "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT   closing.";
RL   BMC Genomics 14:289-289(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003410; AGM04537.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4T0K6; -.
DR   KEGG; aoi:AORI_1949; -.
DR   PATRIC; fig|1156913.3.peg.1996; -.
DR   HOGENOM; CLU_017915_0_0_11; -.
DR   Proteomes; UP000013968; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07328; M48_Ste24p_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..303
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   627 AA;  67767 MW;  2E4F694ECB0DC970 CRC64;
     MQARGRAVLA TLLLVAFPVV VVAVGVASVL AGLRIQGKIG TYVMLGGLAI MVALGFGLMS
     ALRARRPPIE GPRLDREAHP ALWEMIDDLA ALVKTRPPDE IVLIGEINAA VSEDARFLGL
     RPGRRTMLIG LPLLAAMSVS ELRSVLAHEL GHYSGGHTRL LALTYRGTQT LAFTVDRLDG
     GPARALLSAY SKLYLLVARS ANRRQELQAD EASVLAAGSR TAAAALRKVA TLSPLWKDYA
     ERYLSLGAAA RRTPPVLLGF RSYLNHPVQR DWMAEYAEDI IDGEELSKYD SHPPTKRRIA
     ALVGVPDNPV KPDARPGWSL LGAPKIDVPE AELDVLIRDV GPRADWDEVV KRAGRASVAE
     GARLLTAAGI ESRLAPRGTI GEVVRVLRDG DADALAKPLR APSREEGLDL LTELFADTVT
     AAMIDNGVAA HRLNWGGGWE LCLGDGEPFD VTELVGAAVR SPRAVDELVH NLQLLSVPAA
     YFCKQEPQPE PDPAEARMLG MFTALKAKRK LYDLIVCDTE VVLLPLARSV LLRRGLAGLI
     GARGVSDRKR IRKLRERGLD DLRAEPGARR IPFPDIVAGG FPRRKLTTYL TLELSDGETL
     ELAITGNTED FGAAHDELTA FFASLKA
//
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