ID D9QMJ8_BRESC Unreviewed; 946 AA.
AC D9QMJ8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ADL00168.1};
GN OrderedLocusNames=Bresu_0854 {ECO:0000313|EMBL:ADL00168.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL00168.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP002102; ADL00168.1; -; Genomic_DNA.
DR RefSeq; WP_013268271.1; NC_014375.1.
DR AlphaFoldDB; D9QMJ8; -.
DR STRING; 633149.Bresu_0854; -.
DR KEGG; bsb:Bresu_0854; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_007487_1_0_5; -.
DR InParanoid; D9QMJ8; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000002696; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..946
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003127015"
FT DOMAIN 53..163
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..383
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 519..659
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 671..842
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 450..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 99566 MW; C87A6868D456433F CRC64;
MLRSLLLGSS FAVLLAAAPM AASAQNSPDI APPPLEFTHR ELANGLDVYA MPDATAGTVT
VTLWYDVGGK DDPQGRSGFA HLFEHILSRK TINLPYGQIS TIVENAGGSR NASTGQDFTN
YYETVPPQYL ETMLWTHAER MARPVVDEAV FNAERDIVKE ELRQRVYAPP YGRLGVFVIG
DNSYDQSIYR RAVIGSIEEL DSAGIEDARA FHEAYYRPST ATMIVSGNFD PAQLDRWVDQ
YFAGIENPER PLPVLERPVS APRTEPRLVT AYAPNVPLPA IAAIFPGPDA SSDDNAALDV
MGAILSRGQS SRLYRSLVYD KQVAANAFMG SNVEEEAGVV TAQVTVAAGK TVEEAEAALN
AEIARIRDEP VTAAELAEAQ TELLASDLRQ RETSSGRAFM LGQAIVAEHD PRAPDQAVAA
IRAVTIADVQ RVAQKYLDEN ARVSIRYLDD SQRPEGVSED SWKNPATVPT YLSVPPALQA
PNELLPEGQR QAPPAPGEAR PKAAPEIAER TLSNGLRVIV ARSTDLPIMN AQLVIGGGSS
ADPADRPGLA DFTASLASQG AGGRSATEMA RALEGAGANL NSGAGADSST LAVSAPIASA
AVVGDILSDV VENPDFAPAE LERSRTRTVN ALTVALRQPG PLASQVLTRI AYGAAPYGAP
GTGTPASLRA LTREEIEGFH DRWWRPDNAA LIVTGGMTAE EGFAFAERTL GDWARPAGAV
PTVANRAGSA TAPRIVVVDL PGSGQAAVAA AVRGPNRADP SFYPLAVANA VMGGGQGGYL
FQEVRAKRGL SYGAASSLGA RSEAGLITAA TQTKNESALE VLDLVLAQFD RVRTEAPTAA
QVTDRETFAA GNFSRSIETT GGLGGVLAEA VTVGLPLDEA AAYAERVTAT TPETMAAATG
LLNSDQAYVV VVGDSRIFID AMRAAHPDLM LIPAADLDLG SPTLGL
//