ID D0MJ25_RHOM4 Unreviewed; 435 AA.
AC D0MJ25;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:ACY48483.1};
GN OrderedLocusNames=Rmar_1597 {ECO:0000313|EMBL:ACY48483.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48483.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48483.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001807; ACY48483.1; -; Genomic_DNA.
DR AlphaFoldDB; D0MJ25; -.
DR STRING; 518766.Rmar_1597; -.
DR KEGG; rmr:Rmar_1597; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_026846_4_3_10; -.
DR OrthoDB; 9810477at2; -.
DR Proteomes; UP000002221; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 3.10.450.350; -; 2.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR045834; Csd3_N2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF272; BLL1407 PROTEIN; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF19425; Csd3_N2; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..275
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 289..385
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
SQ SEQUENCE 435 AA; 49810 MW; E6324DCA0102F073 CRC64;
MKTPRTVEVK RSVRFFLPLL LVGAAVMALW YIRSRPIDAP SEPARSAVFR PITIVYDAFG
IEEDAFERST HRIRRGETFA DILTRYEVPY ADVLALAEAA RDVFNVRRLQ AGRPFHIYRD
STGARVFVYQ PDPVRYVVFD LRDPVRVYTG RRAVERVLRT AQGVIESSLY ETLQATEADP
ELAIRLSEIF AWQIDFYRIQ RGDRFVALYE ETLIDGEPVG IERVLAARFQ HMGEDFYAFR
FEHDGGVDYY DEAGRNLRKA FLKAPLRYSR ITSRYSLRRF HPVQKRYKPH LGTDYAAPAG
TPVYATGDGV VIEAGYTRYN GYYVKIRHNA VYTTGYLHFS RIAKGIRPGV RVRQGQVIGY
VGSTGLATGP HVCYRFWKNG RQVDPLREQL PPGEPVPDSL RDAFFTLRDR LMPRLLFEPP
AYAEATAAIE GDVTL
//