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Database: UniProt
Entry: F4KMX1_PORAD
LinkDB: F4KMX1_PORAD
Original site: F4KMX1_PORAD 
ID   F4KMX1_PORAD            Unreviewed;       433 AA.
AC   F4KMX1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Peptidase M23 {ECO:0000313|EMBL:AEE13349.1};
GN   OrderedLocusNames=Poras_1416 {ECO:0000313|EMBL:AEE13349.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS   JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE13349.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002689; AEE13349.1; -; Genomic_DNA.
DR   RefSeq; WP_013760721.1; NC_015501.1.
DR   AlphaFoldDB; F4KMX1; -.
DR   STRING; 879243.Poras_1416; -.
DR   KEGG; pah:Poras_1416; -.
DR   eggNOG; COG4942; Bacteria.
DR   HOGENOM; CLU_029425_4_2_10; -.
DR   OrthoDB; 9815884at2; -.
DR   Proteomes; UP000006545; Chromosome.
DR   CDD; cd12797; M23_peptidase; 1.
DR   Gene3D; 6.10.250.3150; -; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR   PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..433
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003311787"
FT   DOMAIN          336..428
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
FT   REGION          259..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          32..66
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   433 AA;  49419 MW;  982CBD150F2E586A CRC64;
     MSHLRRLLYT LCLLTLTGTL LLAQQPKKSA AVRKLERQRT ELLNAIKKTD KEIKSLGQNL
     SEKAKQDKLV RQQIKDRSQV IVLLDQEVAL LNISIDSLAI QIGKLQQKEE VSRERYAKTL
     QALQQRPRFE DRLLFILSAS SFDEGIRRVR YLSAYARAHK EVAAQLHTTR EQLQASQNQL
     IATKQQKGTL LQLRAEERVK LEQQQKSIAS EVKELSTERQ SLQKKLKQQQ RKAEQLNQAI
     QDQIAREIAE AERKAREERE RLEREARKKG KKVPKEAERR AETKDGYAMD AAERKLASSF
     AANKGQLPPP VKGRYRVIRR FGLQQHDDLA MVQTRNGGID IQVARGTEAV AIFDGVVSKV
     FVVPGYHNSI IIRHGNYLTV YANLQNVSVR AGQKVKTGQV LGTVASDDGG QYGVMQFQVW
     HERNKLNPQA WIR
//
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