ID A0A0H5M0H5_YERIN Unreviewed; 311 AA.
AC A0A0H5M0H5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN Name=flgJ_2 {ECO:0000313|EMBL:CRY56974.1};
GN ORFNames=ERS008476_04021 {ECO:0000313|EMBL:CRY56974.1};
OS Yersinia intermedia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=631 {ECO:0000313|EMBL:CRY56974.1, ECO:0000313|Proteomes:UP000043316};
RN [1] {ECO:0000313|Proteomes:UP000043316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R148 {ECO:0000313|Proteomes:UP000043316};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC peptidoglycan layer to assemble the rod structure in the periplasmic
CC space. {ECO:0000256|ARBA:ARBA00002954}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 73 family. {ECO:0000256|ARBA:ARBA00007974}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC {ECO:0000256|ARBA:ARBA00006880}.
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DR EMBL; CWJI01000019; CRY56974.1; -; Genomic_DNA.
DR RefSeq; WP_053010355.1; NZ_CWJI01000019.1.
DR AlphaFoldDB; A0A0H5M0H5; -.
DR Proteomes; UP000043316; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.70.40; peptidoglycan hydrolase; 1.
DR InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR InterPro; IPR013377; FlaJ.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR NCBIfam; TIGR02541; flagell_FlgJ; 1.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:CRY56974.1};
KW Cilium {ECO:0000313|EMBL:CRY56974.1};
KW Flagellum {ECO:0000313|EMBL:CRY56974.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CRY56974.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CRY56974.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT DOMAIN 138..304
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 311 AA; 33306 MW; 14470DFD54FF42DA CRC64;
MSGFNLNQGA AFDLRSLDSL KLAVKNDASQ GAEAAAKQME GLFVQMMLKS MREASFKGGL
LDSPQSDMFT SMYDQQIAQD IASSGKLGFA ELIMSQLTGE KVETGRSTGG IPVELASSLA
NFKGIPVQVT PQSDAPTPAR YSGASSSHSF ISRMLAPAIK AGGQSGIPHQ LIIAQAALES
GWGDREILTK EGKPSHNLFG IKATSAWKGE TTEITTTEYI DGVRQKVKAV FKVYPSYSEA
LADYTSLLSN NPRYKNISQS SSPEIAAKVL QSGGYATDPR YANKLINIIQ QVKQNVGQAV
NAYKTDISSL F
//
