ID A0A1H9LR71_9BURK Unreviewed; 308 AA.
AC A0A1H9LR71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=SAMN02982919_01839 {ECO:0000313|EMBL:SER13991.1};
OS Giesbergeria anulus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Giesbergeria.
OX NCBI_TaxID=180197 {ECO:0000313|EMBL:SER13991.1, ECO:0000313|Proteomes:UP000199766};
RN [1] {ECO:0000313|EMBL:SER13991.1, ECO:0000313|Proteomes:UP000199766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35958 {ECO:0000313|EMBL:SER13991.1,
RC ECO:0000313|Proteomes:UP000199766};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGD01000004; SER13991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LR71; -.
DR STRING; 180197.SAMN02982919_01839; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000199766; 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:SER13991.1};
KW Cilium {ECO:0000313|EMBL:SER13991.1};
KW Flagellum {ECO:0000313|EMBL:SER13991.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000199766}.
FT DOMAIN 146..306
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 308 AA; 32497 MW; 7A4BAC95563F54B7 CRC64;
MALALNPPSS GAALGTNGLA ADARSLNQLK YQAGQNSAEA TKEAAKQFES LFMREMIKSM
REATMKSGLL ESSQADLGTD LLDQQLSVSM SGLPGGLSEA ITRQLSQQMG GASATLAVPS
TLSLARSSQT AAAMRPNAAT SAVANAGPAP KGRDDFVQFH ETAAQRVAQE SGIPASFMLG
QAGHETGWGK SEIRGSDGSN SHNLFGIKAG KGWTGKVAEI VTTEYIDGTP RKVVDKFRAY
DSYEDSFRDY ARLINSSPRY EQARTQTGSA EAYASALQKA GYATDPAYAR KLSGAIQSAL
RAQQRDQA
//
