ID A0A0K6H611_9NEIS Unreviewed; 320 AA.
AC A0A0K6H611;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=Ga0061063_2592 {ECO:0000313|EMBL:CUA86156.1};
OS Gulbenkiania indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Gulbenkiania.
OX NCBI_TaxID=375574 {ECO:0000313|EMBL:CUA86156.1, ECO:0000313|Proteomes:UP000243535};
RN [1] {ECO:0000313|Proteomes:UP000243535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17901 {ECO:0000313|Proteomes:UP000243535};
RA Varghese N.;
RL Submitted (AUG-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; CYHA01000007; CUA86156.1; -; Genomic_DNA.
DR RefSeq; WP_054285331.1; NZ_LION01000007.1.
DR AlphaFoldDB; A0A0K6H611; -.
DR STRING; 375574.GCA_001418035_02368; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000243535; 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:CUA86156.1};
KW Cilium {ECO:0000313|EMBL:CUA86156.1};
KW Flagellum {ECO:0000313|EMBL:CUA86156.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000243535}.
FT DOMAIN 160..319
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 320 AA; 34540 MW; FA6351566B646C2A CRC64;
MSINNAYTRY SSQILGNRLA ADPTAMSDLR LQATRDPKSA VKAVASQFEG LFMNSLMQAM
RTTSLDGEQD SNGMDTYKSL YDQQLVQAMS QRGIGLGDVL TRQLTRFIDK TDKPANVEDA
ALKLEPPRAS SRLQQALQKY GVAQPAEAVG AVVRQAAEAA ARLPSSPREF AASLLPHAQA
AAEKLGVAAE AIVAHAALET GWGRRTIKAA DGTESHNLFG IKAGANWQGD TVKVMTTEYV
NGTPQKRVET FRAYASYSEA LEDYARLLGD NPRYRAALNQ GDNYKGFASA LQTGGYATDP
RYARKLAAVA SRVAQTTIQV
//
