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
//