ID Q2RQ28_RHORT Unreviewed; 459 AA.
AC Q2RQ28;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Peptidase M16-like {ECO:0000313|EMBL:ABC23767.1};
DE EC=3.4.24.64 {ECO:0000313|EMBL:ABC23767.1};
GN OrderedLocusNames=Rru_A2972 {ECO:0000313|EMBL:ABC23767.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC23767.1, ECO:0000313|Proteomes:UP000001929};
RN [1] {ECO:0000313|EMBL:ABC23767.1, ECO:0000313|Proteomes:UP000001929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC {ECO:0000313|Proteomes:UP000001929};
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(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, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000230; ABC23767.1; -; Genomic_DNA.
DR RefSeq; WP_011390720.1; NC_007643.1.
DR RefSeq; YP_428054.1; NC_007643.1.
DR AlphaFoldDB; Q2RQ28; -.
DR STRING; 269796.Rru_A2972; -.
DR MEROPS; M16.019; -.
DR EnsemblBacteria; ABC23767; ABC23767; Rru_A2972.
DR KEGG; rru:Rru_A2972; -.
DR PATRIC; fig|269796.9.peg.3081; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_5; -.
DR PhylomeDB; Q2RQ28; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABC23767.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 49..194
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..388
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 459 AA; 50089 MW; FD0AA45A089CBDE7 CRC64;
MIKRRFGFRG PGSRLGALIV LVVLGLPALA RAQVFNPETF TLPNGMEVVV IPNHRVPVVH
HMVWYKIGAA DEPAGKSGLA HLLEHLMFKG TPTIPPGEFS KIVARNGGQD NAFTSSDFTA
YFQSIAKDRL PMVMEMEADR MANLRLSEED FQTERQVVRE ERRSRTDNEP GELLSERIGQ
ALWGTHPYKN PIIGWEPELM ALTRADALAF YDRYYAPNNA ILVVAGDITA AELKPLAERT
YGALPRRDTP QRASLRDPLR ALPPPAETVI TMHHAQVAQP SFSRRYVAPS AAFDPQGMAD
ALEVLDEILG GGSSGRLYKH LVIERGMAVS AGSWYRGEAL DWGSFGLYAS PRDGVAMADL
VAAVDAEVAS LLDQGVKADE VDDAKRRLTA GLVYARDSLS EGARALGEAL TTGSSVAQVE
SWPERIKAVT PEQVSAAARA VLGRRDRSVT GFLLPEPRS
//