ID   K1EAS4_9MICO            Unreviewed;       447 AA.
AC   K1EAS4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN   ORFNames=B277_01629 {ECO:0000313|EMBL:EKA62537.1};
OS   Janibacter hoylei PVAS-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA62537.1, ECO:0000313|Proteomes:UP000004474};
RN   [1] {ECO:0000313|EMBL:EKA62537.1, ECO:0000313|Proteomes:UP000004474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA62537.1,
RC   ECO:0000313|Proteomes:UP000004474};
RX   PubMed=23144385; DOI=10.1128/JB.01728-12;
RA   Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA   Shouche Y.S.;
RT   "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT   Stratospheric Air.";
RL   J. Bacteriol. 194:6629-6630(2012).
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:EKA62537.1}.
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DR   EMBL; ALWX01000005; EKA62537.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1EAS4; -.
DR   STRING; 1210046.B277_01629; -.
DR   PATRIC; fig|1210046.3.peg.321; -.
DR   eggNOG; COG0771; Bacteria.
DR   OrthoDB; 9803907at2; -.
DR   Proteomes; UP000004474; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR23135:SF7; LIPID II ISOGLUTAMINYL SYNTHASE (GLUTAMINE-HYDROLYZING) SUBUNIT MURT; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE   4: Predicted;
FT   DOMAIN          57..210
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   REGION          241..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48676 MW;  97C4D248DB73619F CRC64;
     MLKTTIAALA GKAARRAARL RGGGTGGSAL PGLVAEKIDP GFLAHALADV PGGIVVVSGT
     NGKTTTTKML VALLRAHGRT VFTNPTGSNF TRGVISAMLS ERLHRGRLQA DIAVLELDEA
     HALHFARAVA PTYALLLNVA RDQLDRFAEI DHTAGLLTQL AGMTTTGVVL NRDDPFVNRI
     ATTVGADVDV TWFGLDASIA DRLGELQEHD ARGHDAWSPP AARARDCLLQ PQDEQRLSVL
     FGEAGEGGAA RPRRAASARA RRDDQRDRSH GHGADPARRG LRPRGRGAGA ADGGPSLRPW
     RGRRRRRDPA RARPRQEPGW LHRRPRHLRL DPRRHDGRDQ RRLRRRPRRL LALRRELRVA
     AGQGGRDHQR CAGLGHGAAP PVRRRAGGLD GGRPRPGPRR LPRRPRRGAQ ADLLHLHRDA
     RAAPHARRAV RPARDGRGRP RDPGSLT
//