ID A0A2I1K8E8_9LACT Unreviewed; 852 AA.
AC A0A2I1K8E8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain-containing protein {ECO:0000259|SMART:SM00047};
GN ORFNames=CYJ27_00220 {ECO:0000313|EMBL:PKY91904.1};
OS Aerococcus christensenii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=87541 {ECO:0000313|EMBL:PKY91904.1, ECO:0000313|Proteomes:UP000234775};
RN [1] {ECO:0000313|EMBL:PKY91904.1, ECO:0000313|Proteomes:UP000234775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0844 {ECO:0000313|EMBL:PKY91904.1,
RC ECO:0000313|Proteomes:UP000234775};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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:PKY91904.1}.
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; PKGZ01000001; PKY91904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1K8E8; -.
DR Proteomes; UP000234775; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.30.30.170; -; 3.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR025987; GW_dom.
DR InterPro; IPR038200; GW_dom_sf.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF13457; GW; 5.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF82057; Prokaryotic SH3-related domain; 3.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000234775};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 509..670
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 27..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 95145 MW; 4FDA69A191F5B6A3 CRC64;
MKPYQKILLA SQAVVAFAVV NQQEQVNAAQ VDKTALSRET TSDSLSVSKE NLEKREVKET
KKSTVTDPKQ KKEGKTQSVS SSEFQDRSVN EKAKQTESSS SKQSIKSVKE ETAQANPMVE
SSQGEVELHY QAEIENEGYT IDTKPWGEEG FHSANVGSSD DYLHQIVYIQ KEDKDGNYAN
VWTKYRELGW IDKRAFKGFT ESTYEARLEF AGYSIDTKPW GTTGYQTKGF TNDYLDSDVK
VVMENETRDY ALVVKNGQEL GWIDKRSLTT YIQPTPTAIV RAGYSVDTKP WGTAGFTLSQ
YGWSEGLLGT PVIIRRVDQS GAYVFITDSN NNGMGWIDRR ALVQNPRNQK AYVTRYGYSL
DTKPWGEEGF KSAGNGTSAD YIGTQVRIID ESGNGAYVFV ASQNQGLGWL DKRALRSIEG
AQSAMIKSPG YSLDTRPWGE EGFHSMGNGT SADYLGSQVR IIDASDNGAY VFVVDSSGKG
LGWLDTRAFR AEELQQIIDK REQETGQSID AVLQPTGNVF LDSILVPAYE LANQNGLYAS
VMLAQAALES GWGRSSLSIP PYYNLFGVKG EYQGNYVSKP TLEDNGSGEY YQIEARFRAY
PSYRESLSDY VNLLKNGLTS NPRFYAPTWK ENTNSYRDAT RYLTGTYATD THYGEKLNAI
IEQFNLTRYD TNVKQGSENQ VAAMNGTVAE WLVNEARDWI GVKMGSERHH ELVDLYNTIT
PLPLNYQLKY NDAWCDAFVT VMAMKANLSS LIGCECGVQR HIDIFKEKGI WYEDGTITPQ
VGDLVAFSWR QNSQPNDNFA DHIGIVESVD PYANTFTTIE GNAGPESKVM RVTYPIGHGN
IRGFARPNYP AF
//
