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Database: UniProt
Entry: L8DQQ0_9NOCA
LinkDB: L8DQQ0_9NOCA
Original site: L8DQQ0_9NOCA 
ID   L8DQQ0_9NOCA            Unreviewed;       529 AA.
AC   L8DQQ0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Putative peptidase/ transglycosylase {ECO:0000313|EMBL:CCQ18327.1};
GN   ORFNames=RHODMAR_4943 {ECO:0000313|EMBL:CCQ18327.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ18327.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ18327.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ18327.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family.
CC       {ECO:0000256|ARBA:ARBA00007074}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCQ18327.1}.
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DR   EMBL; CAPS01000144; CCQ18327.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8DQQ0; -.
DR   STRING; 1268303.RHODMAR_4943; -.
DR   eggNOG; COG0739; Bacteria.
DR   eggNOG; COG0741; Bacteria.
DR   eggNOG; COG0791; Bacteria.
DR   OrthoDB; 9815778at2; -.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd12797; M23_peptidase; 1.
DR   CDD; cd13399; Slt35-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR031304; SLT_2.
DR   PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          408..529
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          55..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  53511 MW;  26BFA9BDCD340EC3 CRC64;
     MTLVAPPETV VSPDSKAPRR WWKLILAVGI AALGVLVVVP LVVIVIVTSS GSNGCAPTVS
     SGTGGEDASP LTPSGPIGKP TRDGTTTMTS PFGQRWGTMH QGVDFAGPIG TPIYAALDGT
     VVKAGPARGF GMWIVLDSIV DGKPVSTVYG HMYPNGVLVK EGQQVKVGNH IADIGNAGGS
     TGPHLHFEYW EGGRLQGGTA IDPMIKLGQA GSPQSAGDGS ATGVGAVVDC GFGTAGGDLR
     AGSVPPEFEP WIRKAGAVCP GVSAPLIASQ LSAENGFKYG PSAPVSSTGA LGPAQFMPGT
     WATWGKDYDG DGRADPNSIG DAVISQAHFM CAINGDITAA IAAGKVKGDP TALTIAGYNA
     GPGAVLAAGG MPSGGDYTTQ TQPYVAKILA GQAQYTSQGS AGRFVPTGAD GDNVVEAARQ
     YLGTPYVWGG GDVNGPSRGG FDCSGLTSFA YFSGKNITLP RTSEAQWGVG SEIPIDQAMP
     GDLVFGSFDA NGPGHVGIYI GDGQMIHAPT TGDVVKQAPL MAGMKARRI
//
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