ID A0A3M8PAR6_9BACL Unreviewed; 482 AA.
AC A0A3M8PAR6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Cell wall hydrolase {ECO:0000313|EMBL:RNF40320.1};
GN ORFNames=EEX84_04935 {ECO:0000313|EMBL:RNF40320.1};
OS Planococcus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1848460 {ECO:0000313|EMBL:RNF40320.1, ECO:0000313|Proteomes:UP000275473};
RN [1] {ECO:0000313|EMBL:RNF40320.1, ECO:0000313|Proteomes:UP000275473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCB217 {ECO:0000313|EMBL:RNF40320.1,
RC ECO:0000313|Proteomes:UP000275473};
RX PubMed=29300160; DOI=10.1099/ijsem.0.002548;
RA Gan L.;
RT "Planococcus salinus sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkali soil.";
RL Int. J. Syst. Evol. Microbiol. 68:589-595(2018).
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:RNF40320.1}.
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DR EMBL; RIAX01000003; RNF40320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8PAR6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000275473; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF08239; SH3_3; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 1.
DR PROSITE; PS51272; SLH; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RNF40320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275473};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018008841"
FT DOMAIN 21..80
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 81..144
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 195..259
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 482 AA; 51726 MW; B26324DD19898B7C CRC64;
MLMLCLMLIA SVLVPLSHAN ASSNFKDVGD THRANAEITY LVDRGIANGV SRTHFVPSKQ
VTRAEAAAML GRALGVNGDR KATRFSDVGG GNMASGYIEE LVKKGIISGY PDGTFGPNKV
LNRGEMAILI NRAFNFGGTS VSSAARNLMD RGIAQGYPDG SFGADAKIIR ADFSVFMARS
INPDFRVKTD GISFSTTMYV NTGSDTLNLR KGPGTTHASI SSLKNGTAVG VASTSGGWSH
IKVNGVIGYV STAYLSVSKP GSVAPSTPPK GASDLTVIID PGHGAHDPGG VGNGFQEKNV
VLNVGRHMKS YFDKTPITAK MTRNSDVFVT LGDRAKFASR NGGDIFVSLH TNALNGSANG
QETFYYAKTA ATNPNVKQSR ALAIYLQARM QETWNLRNRG VNPFGYGNFA VLRNNTVPAA
LIEMGFIDSA TDIQYIKLES QRERMGKALF LATLDYFYHY EGRSDVLPYY NDVNASPSRK
LH
//
