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Database: UniProt
Entry: A0A127JRH8_9BURK
LinkDB: A0A127JRH8_9BURK
Original site: A0A127JRH8_9BURK 
ID   A0A127JRH8_9BURK        Unreviewed;       500 AA.
AC   A0A127JRH8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:AMO22598.1};
GN   ORFNames=UC35_06490 {ECO:0000313|EMBL:AMO22598.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO22598.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO22598.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO22598.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT   description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP010951; AMO22598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A127JRH8; -.
DR   PATRIC; fig|94132.3.peg.1318; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000070433; Chromosome.
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; cd07333; M48C_bepA_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000070433};
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..500
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007449470"
FT   DOMAIN          65..262
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   500 AA;  53258 MW;  BBD57C30F417F6C1 CRC64;
     MSMHPFRPLL LAALLLSACV SQVVNPVTGR TELSAMDEAA EIQEGAKAHQ DVMKEYRAYA
     DPGLQAYVNE VGQKLARQSH RANLKWTFTV LDSPEINAFA LPGGYVYVTR GIMAYLDSEA
     ELAGVMGHEI GHVTARHGAQ RATRQQTAGI GVLAATVLGA VLEAGGVGGA TGLASQVSQT
     AAAGYIASYS RDQESQADEL GAEYLTRNRY NPQNMVEVIQ VLKSQEQFAA DMAKAEGRRV
     PSASNWLSSH PANDKRLADI KAFAAKYKSQ EGYADDGRAR YLQAIAGMAF GDSPEQGLVR
     GRNFYHEGLG IALTAPQGWQ IQNAPEAIAL VNAAGDAGLV VRLVPPKAGN THEEVIRNVL
     KPLDGRIDRR TIHGLAATHF SGTVRNQQGQ TGQVALTLVS GPAGRTYWLQ QAASNADARQ
     RAQAGLMEAE SSFRPMSPAD RAAARPWSVQ AVPYPRGGFG ELAKSTPLPA ERAEAQLKLM
     NGVYGGGADP KPGQAVKVVK
//
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