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Database: UniProt
Entry: A0A268U1A7_9HELI
LinkDB: A0A268U1A7_9HELI
Original site: A0A268U1A7_9HELI 
ID   A0A268U1A7_9HELI        Unreviewed;       479 AA.
AC   A0A268U1A7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=BKH43_04275 {ECO:0000313|EMBL:PAF50779.1};
OS   Helicobacter sp. 13S00401-1.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1905758 {ECO:0000313|EMBL:PAF50779.1, ECO:0000313|Proteomes:UP000216091};
RN   [1] {ECO:0000313|EMBL:PAF50779.1, ECO:0000313|Proteomes:UP000216091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13S00401-1 {ECO:0000313|EMBL:PAF50779.1,
RC   ECO:0000313|Proteomes:UP000216091};
RX   PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA   Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT   "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT   independent niche adaptation followed by diversification in a
RT   poikilothermic host.";
RL   Sci. Rep. 7:8387-8387(2017).
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:PAF50779.1}.
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DR   EMBL; MLAR01000005; PAF50779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268U1A7; -.
DR   Proteomes; UP000216091; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000216091}.
FT   DOMAIN          317..472
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          122..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  54252 MW;  B6B8E14E775E49D3 CRC64;
     MRYILLVVFL FCGLHANNIK FVGAVPFGSS SLRLEANSNL IQTKIKVYRK DSKEVYIDIP
     SRLTFGKKEY KFANKTSITL TQHHTHIVRI SIKLTKTTSY EYRVSGKYFY IEIKDMPVST
     KATTKKQDSI HQTHSTKTKK EQAQREKKSL EKQKEKIKEK LAHKKKEPTK VEPKKLESKK
     PEPKKIESKK IESKKDESNH NHDHHDHQAP IKPVYITPLS AQFAKELHSF AHDKPILISK
     ENYKENQKLP PGSRKKVIVI DPGHGGKDCG TFGIDKVCEK VIVLAIGKKL ASILDRMGYV
     VYMTRDSDVF IDLRRRTEMA NEIKADLFVS IHANSIPKGK PNTPKGIETY FLSTARTERA
     LAVADIENQG DTATMNYFSK SYFLSTINSQ RLVASNKLAI DIQFGALKSV RTKYKDVVDG
     GVREGPFWVL AGALMPSVLI ETGYNSNPIE APRLINNDYQ ELLAIGIANG IRSYFAKNP
//
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