ID F2JKQ6_CELLD Unreviewed; 700 AA.
AC F2JKQ6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ADZ83309.1};
GN OrderedLocusNames=Clole_1584 {ECO:0000313|EMBL:ADZ83309.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ83309.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ83309.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
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DR EMBL; CP002582; ADZ83309.1; -; Genomic_DNA.
DR RefSeq; WP_013656607.1; NC_015275.1.
DR AlphaFoldDB; F2JKQ6; -.
DR STRING; 642492.Clole_1584; -.
DR KEGG; cle:Clole_1584; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_10_0_9; -.
DR Proteomes; UP000008467; Chromosome.
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; 2.60.40.3500; -; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_sf.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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; PF11741; AMIN; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADZ83309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..700
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003279017"
FT DOMAIN 582..694
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 148..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 77474 MW; 90B725B7107A14B3 CRC64;
MSKKLGIMLL AATLFCTNAV PTTAATIVYD GRAHEYNLPA ISLYVNGNKI ATTMDPIQLE
GRVLVPAREV FTPMGAKVSW DAKAKQVTVA YKDTTMLLTV NQKEVWLNGK TVSLDVPAKI
INDKVMIPVR FISEQLGFIV DWNGSNRQVS ITEPTSPPTE EEKPPVEEEP PVEEEKPSIS
NEEYIGTSNK HQIELPSASY SQTKVMEVSV NENNGQHTTF ISAASPISNA KIELQAGKVI
IDIGNSKSQL SNTISPTNNT YIKNIRTSQF TTDTTRVVLD LKSGALVKAG FSEDRSSIMV
QLSNQKIEQI KYMQKNGADT LYYKGLSKDQ IILDYNEKEN LLNFTVPHTT IETTINWTQL
NGRYIDKVTI NGEDNQVKGS IWLKGKVDYQ LTSDYQGATL TLSAYTEVPP VEEVTDSLVY
VSGDNPTIQL FNIPGLNKNA IKVTDDYRNK TLVFDLGKDY SSVLKNNNMV INDTRINKIQ
VATNGTTKIT VVTQKVYAYN FYESDGKISL QMVRPKEKYN QIVVLDAGHG GSDSGAVGNG
LTEKGINYKQ AMALYKLLEA DSQIKVYMTR ETDVYPTLQF RTALANDIEA DLFVSIHNNS
ASASIRGAET LYFPSTTDTR GKQVAQIVQN ALVNKCGMIN RGIKARSDLY VLRTSNMPAI
LIETGFISNS AEAALLNSTA FTNKWAQAIY ESIVESFRFL
//