ID   A0A017RT21_9CLOT        Unreviewed;       769 AA.
AC   A0A017RT21;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=Q428_12620 {ECO:0000313|EMBL:EYE87574.1};
OS   Fervidicella metallireducens AeB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Fervidicella.
OX   NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE87574.1, ECO:0000313|Proteomes:UP000019681};
RN   [1] {ECO:0000313|EMBL:EYE87574.1, ECO:0000313|Proteomes:UP000019681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AeB {ECO:0000313|EMBL:EYE87574.1,
RC   ECO:0000313|Proteomes:UP000019681};
RX   PubMed=24786951;
RA   Patel B.K.;
RT   "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT   Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL   Genome Announc. 2:e00345-14(2014).
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:EYE87574.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AZQP01000048; EYE87574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A017RT21; -.
DR   STRING; 1403537.Q428_12620; -.
DR   OrthoDB; 529831at2; -.
DR   Proteomes; UP000019681; 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; 1.10.101.10; PGBD-like superfamily/PGBD; 4.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 2.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
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; 2.
DR   Pfam; PF01471; PG_binding_1; 4.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF47090; PGBD-like; 4.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019681};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..769
FT                   /note="MurNAc-LAA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001495401"
FT   DOMAIN          589..715
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          186..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          471..548
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        186..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   769 AA;  86253 MW;  593433B46DBA44FF CRC64;
     MLKRLTTTIM ILVFTLSIIS QNVFAFTTLK YGSKGNNVKI LQQKLKDFGY FKGTANGVFG
     NETKNAVIKF QQTKKLKATG TVDEKTWNLL NKGTSSNSTK TTQVNTKENT FKKLEKGMSG
     QEVTALQKKL VELKYIKLNT YGYFGSMTVD AVKAFQKSNN LPPTGIVDKK TWDLIFKTNN
     EVKTTTKVDT TTQKNPSSPN IDNQEQNKPV DTSLKKGCSG EEVTSLQKRL AELKYLNIDN
     YGNFDDKTES AVMEFQKKNN LTVTGTVNNE TKKILFSSEA KPKVETSKED TETKPVEGDN
     VNSQIQIPIT SVLQYGSSGN EVTILQNKLN EQGFNCNISG IFEETTLKAV IDFQNANGLA
     ADGIVTQAVL EKLFIQTVIR EIFVQKNGTP GSLTGKIIII DPGHGFKDPG ASYSGVQEKT
     ITLDIGLRLK RILQEAGATV IMTRDTDGNE GYHSLYYRSA VANNQIIELE IPRLMLEISQ
     IEGKIAEQEK NIETKQKELD NLRQLQNPVD QETISNMEIA LGEAMIALEE TRIKKQELEK
     KIDILNQKKQ TFNYYINNPS YKERYGIMKT TSANNYAVNK DLVEIFDLAK EKYNNDVVFI
     SIHCNATSEK VTKASGIQVY VQKDNDSYYT SYYKNYDYKS RQNLGLSLLQ ELNANTSFSK
     KYTSLYKSNL SVLRENNLAS VLVEVGFLNN PDDRLLLTKE QTREDVAFGL YKGLQKYFNI
     KITGKKIFPV IFYINSSISS SSDSKTFNAL FIGSGEVIST PADFNRLSG
//