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}.
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; 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
//